Nutrient chapter

Molybdenum

Molybdenum. Species, exposure and limitations are retained in each linked claim.

128 recorded mechanisms · 18 availability situations · 5 preserved sources. Draft and verified records are labeled separately.

Read recorded mechanisms Open recursive mind map

The mechanisms

What the sources say this nutrient does, one relationship at a time. Plain wording comes first; the technical statement follows.

Human sulfite oxidase converts sulfite to sulfate in the terminal oxidative step of cysteine catabolism.
Human sulfite oxidase / SUOX → Sulfite / SO3(2-) source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/31127934.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d0efd64e9cde371d0223d63607f5f6b76aada3a628c526f915d9b306c9bef7de", "start_char": 0, "end_char": 1649, "text_sha256": "d0efd64e9cde371d0223d63607f5f6b76aada3a628c526f915d9b306c9bef7de"}
experimental_model
Human SUOX Gly362Ser patient fibroblasts and recombinant enzyme maturation assays
exposure
G362S versus WT protein; Moco reconstitution and molybdate supplementation in culture
limitations
One genotype; in-vitro molybdate rescue is not demonstrated clinical treatment for all SUOX defects.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
SUOX clears sulfite by changing it into sulfate.
primary_references
[mo-p31127934] Impaired mitochondrial maturation of sulfite oxidase in a patient with severe sulfite oxidase deficiency. (2019). https://pubmed.ncbi.nlm.nih.gov/31127934/ DOI: 10.1093/hmg/ddz109
tissue_or_cell_type
Mitochondrial intermembrane space; patient fibroblasts
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 586–597
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human SUOX Gly362Ser patient fibroblasts and recombinant enzyme maturation assays · source_derived_draft · unverified_draft
### mo-suox-reaction Human sulfite oxidase converts sulfite to sulfate in the terminal oxidative step of cysteine catabolism. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: SUOX clears sulfite by changing it into sulfate. organism: Homo sapiens tissue_or_cell_type: Mitochondrial intermembrane space; patient fibroblasts experimental_model: Human SUOX Gly362Ser patient fibroblasts and recombinant enzyme maturation assays limitations: One genotype; in-vitro molybdate rescue is not demonstrated clinical treatment for all SUOX defects. exposure: G362S versus WT protein; Moco reconstitution and molybdate supplementation in culture evidence_span: {"source_cache": "artifacts/molybdenum-research/31127934.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d0efd64e9cde371d0223d63607f5f6b76aada3a628c526f915d9b306c9bef7de", "start_char": 0, "end_char": 1649, "text_sha256": "d0efd64e9cde371d0223d63607f5f6b76aada3a628c526f915d9b306c9bef7de"} [mo-p31127934] Impaired mitochondrial maturation of sulfite oxidase in a patient with severe sulfite oxidase deficiency. (2019). https://pubmed.ncbi.nlm.nih.gov/31127934/ DOI: 10.1093/hmg/ddz109
Complete structured claim and evidence
Recombinant human XDH/XOR catalyzed conversion of xanthine to urate.
Human xanthine oxidoreductase / XDH → Xanthine source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/37713777.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9", "start_char": 0, "end_char": 1655, "text_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9"}
experimental_model
Recombinant human XDH variants with urate, superoxide and NO assays
exposure
Xanthine, oxygen and inorganic nitrite assays
limitations
The 2023 Fig. 6E corrigendum corrects a displayed panel; authors state data and conclusions are unchanged. Enzyme activity is not a clinical benefit or dietary response.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens protein
plain_language
The purine-breakdown pathway uses a molybdenum enzyme to make urate.
primary_references
[mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? (2023). https://pubmed.ncbi.nlm.nih.gov/37713777/ DOI: 10.1016/j.redox.2023.102864
tissue_or_cell_type
Purified human enzyme
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 742–753
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human XDH variants with urate, superoxide and NO assays · source_derived_draft · unverified_draft
### mo-xdh-xanthine Recombinant human XDH/XOR catalyzed conversion of xanthine to urate. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The purine-breakdown pathway uses a molybdenum enzyme to make urate. organism: Homo sapiens protein tissue_or_cell_type: Purified human enzyme experimental_model: Recombinant human XDH variants with urate, superoxide and NO assays limitations: The 2023 Fig. 6E corrigendum corrects a displayed panel; authors state data and conclusions are unchanged. Enzyme activity is not a clinical benefit or dietary response. exposure: Xanthine, oxygen and inorganic nitrite assays evidence_span: {"source_cache": "artifacts/molybdenum-research/37713777.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9", "start_char": 0, "end_char": 1655, "text_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9"} [mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? (2023). https://pubmed.ncbi.nlm.nih.gov/37713777/ DOI: 10.1016/j.redox.2023.102864
Complete structured claim and evidence
Human AOX1 structures and kinetics characterize phthalazine binding and oxidation at its molybdenum active site.
Human aldehyde oxidase 1 / AOX1 → Phthalazine source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/26322824.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0c289f1d166c7335431b4d041963accf22af348b4cac506145f2ccef59ca8188", "start_char": 0, "end_char": 1067, "text_sha256": "0c289f1d166c7335431b4d041963accf22af348b4cac506145f2ccef59ca8188"}
experimental_model
Human AOX1 structures and steady-state kinetics with substrate and inhibitor
exposure
Phthalazine and thioridazine
limitations
Specific xenobiotic chemistry; does not establish broad detoxification benefits from molybdenum supplements.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens protein
plain_language
AOX1 processes certain nitrogen-containing compounds.
primary_references
[mo-p26322824] Structural insights into xenobiotic and inhibitor binding to human aldehyde oxidase. (2015). https://pubmed.ncbi.nlm.nih.gov/26322824/ DOI: 10.1038/nchembio.1895
tissue_or_cell_type
Recombinant purified AOX1
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 833–844
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human AOX1 structures and steady-state kinetics with substrate and inhibitor · source_derived_draft · unverified_draft
### mo-aox-phthalazine Human AOX1 structures and kinetics characterize phthalazine binding and oxidation at its molybdenum active site. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: AOX1 processes certain nitrogen-containing compounds. organism: Homo sapiens protein tissue_or_cell_type: Recombinant purified AOX1 experimental_model: Human AOX1 structures and steady-state kinetics with substrate and inhibitor limitations: Specific xenobiotic chemistry; does not establish broad detoxification benefits from molybdenum supplements. exposure: Phthalazine and thioridazine evidence_span: {"source_cache": "artifacts/molybdenum-research/26322824.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0c289f1d166c7335431b4d041963accf22af348b4cac506145f2ccef59ca8188", "start_char": 0, "end_char": 1067, "text_sha256": "0c289f1d166c7335431b4d041963accf22af348b4cac506145f2ccef59ca8188"} [mo-p26322824] Structural insights into xenobiotic and inhibitor binding to human aldehyde oxidase. (2015). https://pubmed.ncbi.nlm.nih.gov/26322824/ DOI: 10.1038/nchembio.1895
Complete structured claim and evidence
Recombinant human mARC1 reduced N-hydroxylated compounds, including N-hydroxycytosine.
Human mitochondrial amidoxime-reducing component 1 / MTARC1 → N-Hydroxycytosine source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/20861021.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0f430936dcc4701e5d57040edcab4b0418e3c49c59620e0f7d5f54aff41e7877", "start_char": 0, "end_char": 1557, "text_sha256": "0f430936dcc4701e5d57040edcab4b0418e3c49c59620e0f7d5f54aff41e7877"}
experimental_model
Recombinant human mARC1/mARC2 biochemical and spectroscopic reconstitution
exposure
N-hydroxylated substrates; cofactor reconstitution
limitations
The 2010 paper could not identify the Mo-ligating cysteine; later structural/mutagenesis work resolves that point. Its earlier inference is not imported as current fact.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Human proteins expressed in Escherichia coli
plain_language
mARC1 removes oxygen from selected nitrogen-containing molecules.
primary_references
[mo-p20861021] Biochemical and spectroscopic characterization of the human mitochondrial amidoxime reducing components hmARC-1 and hmARC-2 suggests the existence of a new molybdenum enzyme family in eukaryotes. (2010). https://pubmed.ncbi.nlm.nih.gov/20861021/ DOI: 10.1074/jbc.m110.169532
tissue_or_cell_type
Purified enzyme system
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 937–948
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human mARC1/mARC2 biochemical and spectroscopic reconstitution · source_derived_draft · unverified_draft
### mo-marc1-nreduction Recombinant human mARC1 reduced N-hydroxylated compounds, including N-hydroxycytosine. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: mARC1 removes oxygen from selected nitrogen-containing molecules. organism: Human proteins expressed in Escherichia coli tissue_or_cell_type: Purified enzyme system experimental_model: Recombinant human mARC1/mARC2 biochemical and spectroscopic reconstitution limitations: The 2010 paper could not identify the Mo-ligating cysteine; later structural/mutagenesis work resolves that point. Its earlier inference is not imported as current fact. exposure: N-hydroxylated substrates; cofactor reconstitution evidence_span: {"source_cache": "artifacts/molybdenum-research/20861021.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0f430936dcc4701e5d57040edcab4b0418e3c49c59620e0f7d5f54aff41e7877", "start_char": 0, "end_char": 1557, "text_sha256": "0f430936dcc4701e5d57040edcab4b0418e3c49c59620e0f7d5f54aff41e7877"} [mo-p20861021] Biochemical and spectroscopic characterization of the human mitochondrial amidoxime reducing components hmARC-1 and hmARC-2 suggests the existence of a new molybdenum enzyme family in eukaryotes. (2010). https://pubmed.ncbi.nlm.nih.gov/20861021/ DOI: 10.1074/jbc.m110.169532
Complete structured claim and evidence
Recombinant human mARC2 also reduced N-hydroxylated substrates, with specificity differing from mARC1.
Human mitochondrial amidoxime-reducing component 2 / MTARC2 → N-Hydroxycytosine source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/20861021.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0f430936dcc4701e5d57040edcab4b0418e3c49c59620e0f7d5f54aff41e7877", "start_char": 0, "end_char": 1557, "text_sha256": "0f430936dcc4701e5d57040edcab4b0418e3c49c59620e0f7d5f54aff41e7877"}
experimental_model
Recombinant human mARC1/mARC2 biochemical and spectroscopic reconstitution
exposure
N-hydroxylated substrates; cofactor reconstitution
limitations
The 2010 paper could not identify the Mo-ligating cysteine; later structural/mutagenesis work resolves that point. Its earlier inference is not imported as current fact.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Human proteins expressed in Escherichia coli
plain_language
mARC2 is a separate protein with overlapping, but unequal, substrate activity.
primary_references
[mo-p20861021] Biochemical and spectroscopic characterization of the human mitochondrial amidoxime reducing components hmARC-1 and hmARC-2 suggests the existence of a new molybdenum enzyme family in eukaryotes. (2010). https://pubmed.ncbi.nlm.nih.gov/20861021/ DOI: 10.1074/jbc.m110.169532
tissue_or_cell_type
Purified enzyme system
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 950–961
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human mARC1/mARC2 biochemical and spectroscopic reconstitution · source_derived_draft · unverified_draft
### mo-marc2-nreduction Recombinant human mARC2 also reduced N-hydroxylated substrates, with specificity differing from mARC1. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: mARC2 is a separate protein with overlapping, but unequal, substrate activity. organism: Human proteins expressed in Escherichia coli tissue_or_cell_type: Purified enzyme system experimental_model: Recombinant human mARC1/mARC2 biochemical and spectroscopic reconstitution limitations: The 2010 paper could not identify the Mo-ligating cysteine; later structural/mutagenesis work resolves that point. Its earlier inference is not imported as current fact. exposure: N-hydroxylated substrates; cofactor reconstitution evidence_span: {"source_cache": "artifacts/molybdenum-research/20861021.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0f430936dcc4701e5d57040edcab4b0418e3c49c59620e0f7d5f54aff41e7877", "start_char": 0, "end_char": 1557, "text_sha256": "0f430936dcc4701e5d57040edcab4b0418e3c49c59620e0f7d5f54aff41e7877"} [mo-p20861021] Biochemical and spectroscopic characterization of the human mitochondrial amidoxime reducing components hmARC-1 and hmARC-2 suggests the existence of a new molybdenum enzyme family in eukaryotes. (2010). https://pubmed.ncbi.nlm.nih.gov/20861021/ DOI: 10.1074/jbc.m110.169532
Complete structured claim and evidence
MOCS1A and MOCS1B jointly support conversion of GTP to cPMP, the first intermediate of human Moco synthesis.
Human MOCS1A-MOCS1B cPMP synthesis system → Cyclic pyranopterin monophosphate / cPMP source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/31996372.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a88a2e2c4aae83293fa6f1860d10bb41b41c32d1ad79b0b04cd5dd3eb02865c7", "start_char": 0, "end_char": 1846, "text_sha256": "a88a2e2c4aae83293fa6f1860d10bb41b41c32d1ad79b0b04cd5dd3eb02865c7"}
experimental_model
Alternative splicing, fluorescence microscopy, fractionation and mitochondrial targeting of human MOCS1 proteins
exposure
Type I-III MOCS1 splice constructs
limitations
Localization and processing experiments; no dietary iron, SAM or molybdenum intervention.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
The cofactor scaffold is built from GTP before molybdenum is inserted.
primary_references
[mo-p31996372] Alternative splicing of the bicistronic gene molybdenum cofactor synthesis 1 (MOCS1) uncovers a novel mitochondrial protein maturation mechanism. (2020). https://pubmed.ncbi.nlm.nih.gov/31996372/ DOI: 10.1074/jbc.ra119.010720
tissue_or_cell_type
Transfected human-cell localization and mitochondrial matrix
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 274–285
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Alternative splicing, fluorescence microscopy, fractionation and mitochondrial targeting of human MOCS1 proteins · source_derived_draft · unverified_draft
### mo-mocs1-cpmp MOCS1A and MOCS1B jointly support conversion of GTP to cPMP, the first intermediate of human Moco synthesis. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The cofactor scaffold is built from GTP before molybdenum is inserted. organism: Homo sapiens tissue_or_cell_type: Transfected human-cell localization and mitochondrial matrix experimental_model: Alternative splicing, fluorescence microscopy, fractionation and mitochondrial targeting of human MOCS1 proteins limitations: Localization and processing experiments; no dietary iron, SAM or molybdenum intervention. exposure: Type I-III MOCS1 splice constructs evidence_span: {"source_cache": "artifacts/molybdenum-research/31996372.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a88a2e2c4aae83293fa6f1860d10bb41b41c32d1ad79b0b04cd5dd3eb02865c7", "start_char": 0, "end_char": 1846, "text_sha256": "a88a2e2c4aae83293fa6f1860d10bb41b41c32d1ad79b0b04cd5dd3eb02865c7"} [mo-p31996372] Alternative splicing of the bicistronic gene molybdenum cofactor synthesis 1 (MOCS1) uncovers a novel mitochondrial protein maturation mechanism. (2020). https://pubmed.ncbi.nlm.nih.gov/31996372/ DOI: 10.1074/jbc.ra119.010720
Complete structured claim and evidence
Human NFS1 transferred sulfur from L-cysteine through an NFS1-bound persulfide intermediate to the rhodanese-like domain of MOCS3.
Human cysteine desulfurase / NFS1 → L-Cysteine source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/18650437.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8180bd148722e8980ef5acbd4ae4c29a0d9d13da56bbccb91165a5eed4ab6f50", "start_char": 0, "end_char": 1547, "text_sha256": "8180bd148722e8980ef5acbd4ae4c29a0d9d13da56bbccb91165a5eed4ab6f50"}
experimental_model
Purified human NFS1/ISD11 and MOCS3 rhodanese-domain interaction and sulfur-transfer assays
exposure
L-cysteine sulfur-donor assays
limitations
Truncated and heterologously expressed proteins; cell localization was investigated independently in 2013.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Human proteins expressed in Escherichia coli
plain_language
Cysteine supplies sulfur that becomes part of the molybdenum cofactor.
primary_references
[mo-p18650437] A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis. (2008). https://pubmed.ncbi.nlm.nih.gov/18650437/ DOI: 10.1074/jbc.m804064200
tissue_or_cell_type
Purified proteins
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 352–363
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human NFS1/ISD11 and MOCS3 rhodanese-domain interaction and sulfur-transfer assays · source_derived_draft · unverified_draft
### mo-nfs1-sulfur Human NFS1 transferred sulfur from L-cysteine through an NFS1-bound persulfide intermediate to the rhodanese-like domain of MOCS3. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Cysteine supplies sulfur that becomes part of the molybdenum cofactor. organism: Human proteins expressed in Escherichia coli tissue_or_cell_type: Purified proteins experimental_model: Purified human NFS1/ISD11 and MOCS3 rhodanese-domain interaction and sulfur-transfer assays limitations: Truncated and heterologously expressed proteins; cell localization was investigated independently in 2013. exposure: L-cysteine sulfur-donor assays evidence_span: {"source_cache": "artifacts/molybdenum-research/18650437.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8180bd148722e8980ef5acbd4ae4c29a0d9d13da56bbccb91165a5eed4ab6f50", "start_char": 0, "end_char": 1547, "text_sha256": "8180bd148722e8980ef5acbd4ae4c29a0d9d13da56bbccb91165a5eed4ab6f50"} [mo-p18650437] A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis. (2008). https://pubmed.ncbi.nlm.nih.gov/18650437/ DOI: 10.1074/jbc.m804064200
Complete structured claim and evidence
MOCS3 activates MOCS2A by adenylation followed by sulfur transfer, forming its C-terminal thiocarboxylate.
Human adenylyltransferase and sulfurtransferase / MOCS3 → Human molybdopterin synthase sulfur carrier / MOCS2A source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/22453920.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "700833295a22a72be9d0ee74144bfe9249d6266c7fcba7b48330a4b2f2bf9c64", "start_char": 0, "end_char": 1267, "text_sha256": "700833295a22a72be9d0ee74144bfe9249d6266c7fcba7b48330a4b2f2bf9c64"}
experimental_model
Human-cell interaction/localization and purified-protein adenylation/sulfuration
exposure
MOCS2A and URM1 terminal glycine variants
limitations
Shared enzyme does not prove competition for sulfur in ordinary nutrient deficiency.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
ATP-driven activation reloads the sulfur carrier.
primary_references
[mo-p22453920] Dual role of the molybdenum cofactor biosynthesis protein MOCS3 in tRNA thiolation and molybdenum cofactor biosynthesis in humans. (2012). https://pubmed.ncbi.nlm.nih.gov/22453920/ DOI: 10.1074/jbc.m112.351429
tissue_or_cell_type
Cytosolic sulfur-transfer pathways
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 443–454
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human-cell interaction/localization and purified-protein adenylation/sulfuration · source_derived_draft · unverified_draft
### mo-mocs3-activate MOCS3 activates MOCS2A by adenylation followed by sulfur transfer, forming its C-terminal thiocarboxylate. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: ATP-driven activation reloads the sulfur carrier. organism: Homo sapiens tissue_or_cell_type: Cytosolic sulfur-transfer pathways experimental_model: Human-cell interaction/localization and purified-protein adenylation/sulfuration limitations: Shared enzyme does not prove competition for sulfur in ordinary nutrient deficiency. exposure: MOCS2A and URM1 terminal glycine variants evidence_span: {"source_cache": "artifacts/molybdenum-research/22453920.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "700833295a22a72be9d0ee74144bfe9249d6266c7fcba7b48330a4b2f2bf9c64", "start_char": 0, "end_char": 1267, "text_sha256": "700833295a22a72be9d0ee74144bfe9249d6266c7fcba7b48330a4b2f2bf9c64"} [mo-p22453920] Dual role of the molybdenum cofactor biosynthesis protein MOCS3 in tRNA thiolation and molybdenum cofactor biosynthesis in humans. (2012). https://pubmed.ncbi.nlm.nih.gov/22453920/ DOI: 10.1074/jbc.m112.351429
Complete structured claim and evidence
Human MOCS2A and MOCS2B assemble as active MPT synthase and convert cPMP to molybdopterin.
Human MOCS2A-MOCS2B molybdopterin synthase → Cyclic pyranopterin monophosphate / cPMP source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/12732628.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319", "start_char": 0, "end_char": 1322, "text_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319"}
experimental_model
Purified human MPT synthase and patient-derived point mutants
exposure
Precursor Z/cPMP conversion assays
limitations
In-vitro assembly and kinetic defects; severity comparisons refer to specific patients, not a universal hierarchy.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Human proteins expressed in Escherichia coli
plain_language
Two sulfur atoms create the part of the scaffold that will hold molybdenum.
primary_references
[mo-p12732628] Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. (2003). https://pubmed.ncbi.nlm.nih.gov/12732628/ DOI: 10.1074/jbc.m303092200
tissue_or_cell_type
Reconstituted MOCS2A/MOCS2B tetramers
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 391–402
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human MPT synthase and patient-derived point mutants · source_derived_draft · unverified_draft
### mo-mpt-synthase Human MOCS2A and MOCS2B assemble as active MPT synthase and convert cPMP to molybdopterin. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Two sulfur atoms create the part of the scaffold that will hold molybdenum. organism: Human proteins expressed in Escherichia coli tissue_or_cell_type: Reconstituted MOCS2A/MOCS2B tetramers experimental_model: Purified human MPT synthase and patient-derived point mutants limitations: In-vitro assembly and kinetic defects; severity comparisons refer to specific patients, not a universal hierarchy. exposure: Precursor Z/cPMP conversion assays evidence_span: {"source_cache": "artifacts/molybdenum-research/12732628.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319", "start_char": 0, "end_char": 1322, "text_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319"} [mo-p12732628] Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. (2003). https://pubmed.ncbi.nlm.nih.gov/12732628/ DOI: 10.1074/jbc.m303092200
Complete structured claim and evidence
The gephyrin G domain produces adenylylated molybdopterin.
Mammalian gephyrin G domain → Metal-free molybdopterin / MPT source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/23163752.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "909388cf5fb7bfa5d2f8444644e20773a7a8ec6a19b4ccb8a4bda78d9ad17c5d", "start_char": 0, "end_char": 1489, "text_sha256": "909388cf5fb7bfa5d2f8444644e20773a7a8ec6a19b4ccb8a4bda78d9ad17c5d"}
experimental_model
Purified mammalian gephyrin domains and full multidomain protein; in-vitro Moco reconstitution
exposure
MPT adenylation, molybdate insertion and domain-combination assays
limitations
No human dietary magnesium intervention; purified domain kinetics should not be turned into supplementation efficacy.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Mammalian protein system
plain_language
Gephyrin prepares the scaffold for metal insertion.
primary_references
[mo-p23163752] Metal insertion into the molybdenum cofactor: product-substrate channelling demonstrates the functional origin of domain fusion in gephyrin. (2013). https://pubmed.ncbi.nlm.nih.gov/23163752/ DOI: 10.1042/bj20121078
tissue_or_cell_type
Purified gephyrin
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 482–493
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified mammalian gephyrin domains and full multidomain protein; in-vitro Moco reconstitution · source_derived_draft · unverified_draft
### mo-gphn-adenylation The gephyrin G domain produces adenylylated molybdopterin. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Gephyrin prepares the scaffold for metal insertion. organism: Mammalian protein system tissue_or_cell_type: Purified gephyrin experimental_model: Purified mammalian gephyrin domains and full multidomain protein; in-vitro Moco reconstitution limitations: No human dietary magnesium intervention; purified domain kinetics should not be turned into supplementation efficacy. exposure: MPT adenylation, molybdate insertion and domain-combination assays evidence_span: {"source_cache": "artifacts/molybdenum-research/23163752.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "909388cf5fb7bfa5d2f8444644e20773a7a8ec6a19b4ccb8a4bda78d9ad17c5d", "start_char": 0, "end_char": 1489, "text_sha256": "909388cf5fb7bfa5d2f8444644e20773a7a8ec6a19b4ccb8a4bda78d9ad17c5d"} [mo-p23163752] Metal insertion into the molybdenum cofactor: product-substrate channelling demonstrates the functional origin of domain fusion in gephyrin. (2013). https://pubmed.ncbi.nlm.nih.gov/23163752/ DOI: 10.1042/bj20121078
Complete structured claim and evidence
The gephyrin E domain catalyzes molybdate incorporation during ATP-dependent Moco synthesis.
Mammalian gephyrin E domain → Molybdate / MoO4(2-) source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/23163752.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "909388cf5fb7bfa5d2f8444644e20773a7a8ec6a19b4ccb8a4bda78d9ad17c5d", "start_char": 0, "end_char": 1489, "text_sha256": "909388cf5fb7bfa5d2f8444644e20773a7a8ec6a19b4ccb8a4bda78d9ad17c5d"}
experimental_model
Purified mammalian gephyrin domains and full multidomain protein; in-vitro Moco reconstitution
exposure
MPT adenylation, molybdate insertion and domain-combination assays
limitations
No human dietary magnesium intervention; purified domain kinetics should not be turned into supplementation efficacy.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Mammalian protein system
plain_language
Molybdenum becomes useful to these enzymes only after being inserted into its cofactor.
primary_references
[mo-p23163752] Metal insertion into the molybdenum cofactor: product-substrate channelling demonstrates the functional origin of domain fusion in gephyrin. (2013). https://pubmed.ncbi.nlm.nih.gov/23163752/ DOI: 10.1042/bj20121078
tissue_or_cell_type
Purified gephyrin
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 495–506
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified mammalian gephyrin domains and full multidomain protein; in-vitro Moco reconstitution · source_derived_draft · unverified_draft
### mo-gphn-insertion The gephyrin E domain catalyzes molybdate incorporation during ATP-dependent Moco synthesis. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Molybdenum becomes useful to these enzymes only after being inserted into its cofactor. organism: Mammalian protein system tissue_or_cell_type: Purified gephyrin experimental_model: Purified mammalian gephyrin domains and full multidomain protein; in-vitro Moco reconstitution limitations: No human dietary magnesium intervention; purified domain kinetics should not be turned into supplementation efficacy. exposure: MPT adenylation, molybdate insertion and domain-combination assays evidence_span: {"source_cache": "artifacts/molybdenum-research/23163752.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "909388cf5fb7bfa5d2f8444644e20773a7a8ec6a19b4ccb8a4bda78d9ad17c5d", "start_char": 0, "end_char": 1489, "text_sha256": "909388cf5fb7bfa5d2f8444644e20773a7a8ec6a19b4ccb8a4bda78d9ad17c5d"} [mo-p23163752] Metal insertion into the molybdenum cofactor: product-substrate channelling demonstrates the functional origin of domain fusion in gephyrin. (2013). https://pubmed.ncbi.nlm.nih.gov/23163752/ DOI: 10.1042/bj20121078
Complete structured claim and evidence
MOCOS defects in type II xanthinuria support its role in supplying the terminal sulfur required by XDH and AOX1.
Human molybdenum cofactor sulfurase / MOCOS → Human xanthine oxidoreductase / XDH source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/11302742.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8f595c96d16b055cd6b9611c4d036626222ffb084ec778f840255cac57ecdfb3", "start_char": 0, "end_char": 1011, "text_sha256": "8f595c96d16b055cd6b9611c4d036626222ffb084ec778f840255cac57ecdfb3"}
experimental_model
Gene identification in two type II xanthinuria patients and comparison subjects
exposure
MOCOS Arg419 stop mutation
limitations
Genetic evidence for terminal sulfuration; type II xanthinuria is different from loss of all Moco synthesis.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
Two molybdenum enzymes need an additional sulfur-activation step.
primary_references
[mo-p11302742] Mutation of human molybdenum cofactor sulfurase gene is responsible for classical xanthinuria type II. (2001). https://pubmed.ncbi.nlm.nih.gov/11302742/ DOI: 10.1006/bbrc.2001.4719
tissue_or_cell_type
Liver cDNA and patient genetics
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 521–532
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Gene identification in two type II xanthinuria patients and comparison subjects · source_derived_draft · unverified_draft
### mo-mocos-sulfuration MOCOS defects in type II xanthinuria support its role in supplying the terminal sulfur required by XDH and AOX1. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Two molybdenum enzymes need an additional sulfur-activation step. organism: Homo sapiens tissue_or_cell_type: Liver cDNA and patient genetics experimental_model: Gene identification in two type II xanthinuria patients and comparison subjects limitations: Genetic evidence for terminal sulfuration; type II xanthinuria is different from loss of all Moco synthesis. exposure: MOCOS Arg419 stop mutation evidence_span: {"source_cache": "artifacts/molybdenum-research/11302742.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8f595c96d16b055cd6b9611c4d036626222ffb084ec778f840255cac57ecdfb3", "start_char": 0, "end_char": 1011, "text_sha256": "8f595c96d16b055cd6b9611c4d036626222ffb084ec778f840255cac57ecdfb3"} [mo-p11302742] Mutation of human molybdenum cofactor sulfurase gene is responsible for classical xanthinuria type II. (2001). https://pubmed.ncbi.nlm.nih.gov/11302742/ DOI: 10.1006/bbrc.2001.4719
Complete structured claim and evidence
Measured molybdenum absorption was 88-93% across the five controlled dietary intakes.
Molybdenum → Intestinal molybdenum absorption source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/7572711.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5f16c3a9bbe66f2f03456d8d374ccaf6ad6af8ddede86d662529567ce840f96e", "start_char": 0, "end_char": 1336, "text_sha256": "5f16c3a9bbe66f2f03456d8d374ccaf6ad6af8ddede86d662529567ce840f96e"}
experimental_model
Stable-isotope balance study, four young men, five 24-day intake periods
exposure
22-1490 micrograms molybdenum/day
limitations
Small short study in healthy young men; absence of observed harm is not a population safety limit.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
Most of the molybdenum in these controlled diets was absorbed.
primary_references
[mo-p7572711] Molybdenum absorption, excretion, and retention studied with stable isotopes in young men at five intakes of dietary molybdenum. (1995). https://pubmed.ncbi.nlm.nih.gov/7572711/ DOI: 10.1093/ajcn/62.4.790
tissue_or_cell_type
Whole-body absorption, urine and feces
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 118–129
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Stable-isotope balance study, four young men, five 24-day intake periods · source_derived_draft · unverified_draft
### mo-absorption Measured molybdenum absorption was 88-93% across the five controlled dietary intakes. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Most of the molybdenum in these controlled diets was absorbed. organism: Homo sapiens tissue_or_cell_type: Whole-body absorption, urine and feces experimental_model: Stable-isotope balance study, four young men, five 24-day intake periods limitations: Small short study in healthy young men; absence of observed harm is not a population safety limit. exposure: 22-1490 micrograms molybdenum/day evidence_span: {"source_cache": "artifacts/molybdenum-research/7572711.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5f16c3a9bbe66f2f03456d8d374ccaf6ad6af8ddede86d662529567ce840f96e", "start_char": 0, "end_char": 1336, "text_sha256": "5f16c3a9bbe66f2f03456d8d374ccaf6ad6af8ddede86d662529567ce840f96e"} [mo-p7572711] Molybdenum absorption, excretion, and retention studied with stable isotopes in young men at five intakes of dietary molybdenum. (1995). https://pubmed.ncbi.nlm.nih.gov/7572711/ DOI: 10.1093/ajcn/62.4.790
Complete structured claim and evidence
Both the amount and percentage of molybdenum excreted in urine rose with dietary intake.
Molybdenum → Urinary molybdenum excretion source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/7572711.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5f16c3a9bbe66f2f03456d8d374ccaf6ad6af8ddede86d662529567ce840f96e", "start_char": 0, "end_char": 1336, "text_sha256": "5f16c3a9bbe66f2f03456d8d374ccaf6ad6af8ddede86d662529567ce840f96e"}
experimental_model
Stable-isotope balance study, four young men, five 24-day intake periods
exposure
22-1490 micrograms molybdenum/day
limitations
Small short study in healthy young men; absence of observed harm is not a population safety limit.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
The kidneys released more molybdenum when more was supplied.
primary_references
[mo-p7572711] Molybdenum absorption, excretion, and retention studied with stable isotopes in young men at five intakes of dietary molybdenum. (1995). https://pubmed.ncbi.nlm.nih.gov/7572711/ DOI: 10.1093/ajcn/62.4.790
tissue_or_cell_type
Whole-body absorption, urine and feces
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 131–142
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Stable-isotope balance study, four young men, five 24-day intake periods · source_derived_draft · unverified_draft
### mo-urinary-control Both the amount and percentage of molybdenum excreted in urine rose with dietary intake. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The kidneys released more molybdenum when more was supplied. organism: Homo sapiens tissue_or_cell_type: Whole-body absorption, urine and feces experimental_model: Stable-isotope balance study, four young men, five 24-day intake periods limitations: Small short study in healthy young men; absence of observed harm is not a population safety limit. exposure: 22-1490 micrograms molybdenum/day evidence_span: {"source_cache": "artifacts/molybdenum-research/7572711.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5f16c3a9bbe66f2f03456d8d374ccaf6ad6af8ddede86d662529567ce840f96e", "start_char": 0, "end_char": 1336, "text_sha256": "5f16c3a9bbe66f2f03456d8d374ccaf6ad6af8ddede86d662529567ce840f96e"} [mo-p7572711] Molybdenum absorption, excretion, and retention studied with stable isotopes in young men at five intakes of dietary molybdenum. (1995). https://pubmed.ncbi.nlm.nih.gov/7572711/ DOI: 10.1093/ajcn/62.4.790
Complete structured claim and evidence
At 22 micrograms/day, molybdenum turnover slowed and balance improved with time, although balance was not consistently achieved.
Molybdenum → Human molybdenum balance source_derived_draftungraded
Experimental context and source evidence
availability_state
nutrient_deficiency Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/7733035.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a566c89562d46c98608ced96cc37d0e248deede57a8164ed8bb993c2d8818bc6", "start_char": 0, "end_char": 1265, "text_sha256": "a566c89562d46c98608ced96cc37d0e248deede57a8164ed8bb993c2d8818bc6"}
experimental_model
Stable-isotope depletion/repletion study in four young men
exposure
22 micrograms/day for 102 days, then 467 micrograms/day for 18 days
limitations
Negative balance is not the same as symptomatic deficiency; requirement estimates are specific to this small cohort.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
The body conserved molybdenum during prolonged low intake.
primary_references
[mo-p7733035] Molybdenum absorption, excretion, and retention studied with stable isotopes in young men during depletion and repletion. (1995). https://pubmed.ncbi.nlm.nih.gov/7733035/ DOI: 10.1093/ajcn/61.4.1102
tissue_or_cell_type
Whole-body molybdenum balance
trigger_kind
nutrient_deficiency Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 144–155
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Stable-isotope depletion/repletion study in four young men · source_derived_draft · unverified_draft
### mo-low-intake-conservation At 22 micrograms/day, molybdenum turnover slowed and balance improved with time, although balance was not consistently achieved. Condition category: nutrient_deficiency nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The body conserved molybdenum during prolonged low intake. organism: Homo sapiens tissue_or_cell_type: Whole-body molybdenum balance experimental_model: Stable-isotope depletion/repletion study in four young men limitations: Negative balance is not the same as symptomatic deficiency; requirement estimates are specific to this small cohort. exposure: 22 micrograms/day for 102 days, then 467 micrograms/day for 18 days evidence_span: {"source_cache": "artifacts/molybdenum-research/7733035.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a566c89562d46c98608ced96cc37d0e248deede57a8164ed8bb993c2d8818bc6", "start_char": 0, "end_char": 1265, "text_sha256": "a566c89562d46c98608ced96cc37d0e248deede57a8164ed8bb993c2d8818bc6"} [mo-p7733035] Molybdenum absorption, excretion, and retention studied with stable isotopes in young men during depletion and repletion. (1995). https://pubmed.ncbi.nlm.nih.gov/7733035/ DOI: 10.1093/ajcn/61.4.1102
Complete structured claim and evidence
No clinical signs of molybdenum deficiency were observed during the 102-day low-intake phase.
Molybdenum → Human molybdenum balance source_derived_draftungraded
Experimental context and source evidence
availability_state
nutrient_deficiency Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/7733035.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a566c89562d46c98608ced96cc37d0e248deede57a8164ed8bb993c2d8818bc6", "start_char": 0, "end_char": 1265, "text_sha256": "a566c89562d46c98608ced96cc37d0e248deede57a8164ed8bb993c2d8818bc6"}
experimental_model
Stable-isotope depletion/repletion study in four young men
exposure
22 micrograms/day for 102 days, then 467 micrograms/day for 18 days
limitations
Negative balance is not the same as symptomatic deficiency; requirement estimates are specific to this small cohort.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
Low intake in this experiment did not produce the severe genetic-deficiency syndrome.
primary_references
[mo-p7733035] Molybdenum absorption, excretion, and retention studied with stable isotopes in young men during depletion and repletion. (1995). https://pubmed.ncbi.nlm.nih.gov/7733035/ DOI: 10.1093/ajcn/61.4.1102
tissue_or_cell_type
Whole-body molybdenum balance
trigger_kind
nutrient_deficiency Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 157–168
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Stable-isotope depletion/repletion study in four young men · source_derived_draft · unverified_draft
### mo-low-intake-no-syndrome No clinical signs of molybdenum deficiency were observed during the 102-day low-intake phase. Condition category: nutrient_deficiency nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Low intake in this experiment did not produce the severe genetic-deficiency syndrome. organism: Homo sapiens tissue_or_cell_type: Whole-body molybdenum balance experimental_model: Stable-isotope depletion/repletion study in four young men limitations: Negative balance is not the same as symptomatic deficiency; requirement estimates are specific to this small cohort. exposure: 22 micrograms/day for 102 days, then 467 micrograms/day for 18 days evidence_span: {"source_cache": "artifacts/molybdenum-research/7733035.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a566c89562d46c98608ced96cc37d0e248deede57a8164ed8bb993c2d8818bc6", "start_char": 0, "end_char": 1265, "text_sha256": "a566c89562d46c98608ced96cc37d0e248deede57a8164ed8bb993c2d8818bc6"} [mo-p7733035] Molybdenum absorption, excretion, and retention studied with stable isotopes in young men during depletion and repletion. (1995). https://pubmed.ncbi.nlm.nih.gov/7733035/ DOI: 10.1093/ajcn/61.4.1102
Complete structured claim and evidence
Modeled fractional tissue storage was lower during repletion than during depletion, while urinary elimination increased.
Molybdenum → Fractional molybdenum tissue retention source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/16549456.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7c6337cd055a31e872ec0f2b24ea7419d5263cdcc6285cbc635e1ffe8f692468", "start_char": 0, "end_char": 1679, "text_sha256": "7c6337cd055a31e872ec0f2b24ea7419d5263cdcc6285cbc635e1ffe8f692468"}
experimental_model
Compartmental reanalysis of four-man depletion/repletion tracer experiment
exposure
102 days at 22 micrograms/day; 18 days at 467 micrograms/day
limitations
Model estimates and adaptations, not an independent clinical trial or universal blood threshold.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
Higher intake did not translate proportionally into more tissue storage.
primary_references
[mo-p16549456] Molybdenum kinetics in men differ during molybdenum depletion and repletion. (2006). https://pubmed.ncbi.nlm.nih.gov/16549456/ DOI: 10.1093/jn/136.4.953
tissue_or_cell_type
Plasma, urine, feces and modeled tissue pools
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 170–181
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Compartmental reanalysis of four-man depletion/repletion tracer experiment · source_derived_draft · unverified_draft
### mo-fractional-retention Modeled fractional tissue storage was lower during repletion than during depletion, while urinary elimination increased. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Higher intake did not translate proportionally into more tissue storage. organism: Homo sapiens tissue_or_cell_type: Plasma, urine, feces and modeled tissue pools experimental_model: Compartmental reanalysis of four-man depletion/repletion tracer experiment limitations: Model estimates and adaptations, not an independent clinical trial or universal blood threshold. exposure: 102 days at 22 micrograms/day; 18 days at 467 micrograms/day evidence_span: {"source_cache": "artifacts/molybdenum-research/16549456.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7c6337cd055a31e872ec0f2b24ea7419d5263cdcc6285cbc635e1ffe8f692468", "start_char": 0, "end_char": 1679, "text_sha256": "7c6337cd055a31e872ec0f2b24ea7419d5263cdcc6285cbc635e1ffe8f692468"} [mo-p16549456] Molybdenum kinetics in men differ during molybdenum depletion and repletion. (2006). https://pubmed.ncbi.nlm.nih.gov/16549456/ DOI: 10.1093/jn/136.4.953
Complete structured claim and evidence
The compartmental model estimated food-bound molybdenum to be approximately 16% less bioavailable than purified molybdenum.
Molybdenum → Intestinal molybdenum absorption source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/16549456.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7c6337cd055a31e872ec0f2b24ea7419d5263cdcc6285cbc635e1ffe8f692468", "start_char": 0, "end_char": 1679, "text_sha256": "7c6337cd055a31e872ec0f2b24ea7419d5263cdcc6285cbc635e1ffe8f692468"}
experimental_model
Compartmental reanalysis of four-man depletion/repletion tracer experiment
exposure
102 days at 22 micrograms/day; 18 days at 467 micrograms/day
limitations
Model estimates and adaptations, not an independent clinical trial or universal blood threshold.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
Chemical form and the food matrix affected the modeled amount available.
primary_references
[mo-p16549456] Molybdenum kinetics in men differ during molybdenum depletion and repletion. (2006). https://pubmed.ncbi.nlm.nih.gov/16549456/ DOI: 10.1093/jn/136.4.953
tissue_or_cell_type
Plasma, urine, feces and modeled tissue pools
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 183–194
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Compartmental reanalysis of four-man depletion/repletion tracer experiment · source_derived_draft · unverified_draft
### mo-food-bioavailability The compartmental model estimated food-bound molybdenum to be approximately 16% less bioavailable than purified molybdenum. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Chemical form and the food matrix affected the modeled amount available. organism: Homo sapiens tissue_or_cell_type: Plasma, urine, feces and modeled tissue pools experimental_model: Compartmental reanalysis of four-man depletion/repletion tracer experiment limitations: Model estimates and adaptations, not an independent clinical trial or universal blood threshold. exposure: 102 days at 22 micrograms/day; 18 days at 467 micrograms/day evidence_span: {"source_cache": "artifacts/molybdenum-research/16549456.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7c6337cd055a31e872ec0f2b24ea7419d5263cdcc6285cbc635e1ffe8f692468", "start_char": 0, "end_char": 1679, "text_sha256": "7c6337cd055a31e872ec0f2b24ea7419d5263cdcc6285cbc635e1ffe8f692468"} [mo-p16549456] Molybdenum kinetics in men differ during molybdenum depletion and repletion. (2006). https://pubmed.ncbi.nlm.nih.gov/16549456/ DOI: 10.1093/jn/136.4.953
Complete structured claim and evidence
Human HsMOT2/MFSD5 expression supported molybdate uptake in yeast, with an apparent affinity near 550 nM.
Human MFSD5 / HsMOT2 → Molybdate / MoO4(2-) source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/21464289.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d2ba286dba58f70f8a9e9a4f61259329ed5f458d5c4b1e9cd13c64df916f300d", "start_char": 0, "end_char": 1707, "text_sha256": "d2ba286dba58f70f8a9e9a4f61259329ed5f458d5c4b1e9cd13c64df916f300d"}
experimental_model
Human HsMOT2 expressed in Saccharomyces cerevisiae, with separate algal experiments
exposure
Molybdate uptake assays and oxyanion comparisons
limitations
Establishes transport capacity in yeast; does not identify the dominant intestinal or renal transporter in people.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Human protein in yeast; Chlamydomonas experiments separately
plain_language
A human protein can carry molybdate when tested in yeast.
primary_references
[mo-p21464289] Algae and humans share a molybdate transporter. (2011). https://pubmed.ncbi.nlm.nih.gov/21464289/ DOI: 10.1073/pnas.1100700108
tissue_or_cell_type
Heterologous membrane transport
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 196–207
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human HsMOT2 expressed in Saccharomyces cerevisiae, with separate algal experiments · source_derived_draft · unverified_draft
### mo-mfsd5-uptake Human HsMOT2/MFSD5 expression supported molybdate uptake in yeast, with an apparent affinity near 550 nM. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: A human protein can carry molybdate when tested in yeast. organism: Human protein in yeast; Chlamydomonas experiments separately tissue_or_cell_type: Heterologous membrane transport experimental_model: Human HsMOT2 expressed in Saccharomyces cerevisiae, with separate algal experiments limitations: Establishes transport capacity in yeast; does not identify the dominant intestinal or renal transporter in people. exposure: Molybdate uptake assays and oxyanion comparisons evidence_span: {"source_cache": "artifacts/molybdenum-research/21464289.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d2ba286dba58f70f8a9e9a4f61259329ed5f458d5c4b1e9cd13c64df916f300d", "start_char": 0, "end_char": 1707, "text_sha256": "d2ba286dba58f70f8a9e9a4f61259329ed5f458d5c4b1e9cd13c64df916f300d"} [mo-p21464289] Algae and humans share a molybdate transporter. (2011). https://pubmed.ncbi.nlm.nih.gov/21464289/ DOI: 10.1073/pnas.1100700108
Complete structured claim and evidence
Tungstate inhibited HsMOT2-dependent molybdate uptake in yeast; 1 mM sulfate had little effect.
Tungstate / WO4(2-) → Human MFSD5 / HsMOT2 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/21464289.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "861076d0403540a9fe3ad941cd7c0807224cb9323da6d8179546e9983f782cc7", "start_char": 18693, "end_char": 18917, "text_sha256": "df769097827247aa8c9b82a5877b016a6977021d43424f2deed3aad684c51688"}
experimental_model
Human HsMOT2 expressed in Saccharomyces cerevisiae, with separate algal experiments
exposure
Molybdate uptake assays and oxyanion comparisons
limitations
The text and figure use different tungstate concentrations; no exact tungstate dose is assigned here. Yeast assay, not human dietary competition.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Human protein in yeast; Chlamydomonas experiments separately
plain_language
Tungstate competed in this transporter assay, while sulfate had little effect.
primary_references
[mo-p21464289] Algae and humans share a molybdate transporter. (2011). https://pubmed.ncbi.nlm.nih.gov/21464289/ DOI: 10.1073/pnas.1100700108
tissue_or_cell_type
Heterologous membrane transport
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 209–220
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human HsMOT2 expressed in Saccharomyces cerevisiae, with separate algal experiments · source_derived_draft · unverified_draft
### mo-tungstate-transport Tungstate inhibited HsMOT2-dependent molybdate uptake in yeast; 1 mM sulfate had little effect. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Tungstate competed in this transporter assay, while sulfate had little effect. organism: Human protein in yeast; Chlamydomonas experiments separately tissue_or_cell_type: Heterologous membrane transport experimental_model: Human HsMOT2 expressed in Saccharomyces cerevisiae, with separate algal experiments limitations: The text and figure use different tungstate concentrations; no exact tungstate dose is assigned here. Yeast assay, not human dietary competition. exposure: Molybdate uptake assays and oxyanion comparisons evidence_span: {"source_cache": "artifacts/molybdenum-research/21464289.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "861076d0403540a9fe3ad941cd7c0807224cb9323da6d8179546e9983f782cc7", "start_char": 18693, "end_char": 18917, "text_sha256": "df769097827247aa8c9b82a5877b016a6977021d43424f2deed3aad684c51688"} [mo-p21464289] Algae and humans share a molybdate transporter. (2011). https://pubmed.ncbi.nlm.nih.gov/21464289/ DOI: 10.1073/pnas.1100700108
Complete structured claim and evidence
Large HsMOT2/MFSD5 overexpression increased the molybdate-sensitive FRET signal in HEK-293T cells.
Human MFSD5 / HsMOT2 → Cellular molybdate uptake source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/23472155.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a3c76154f22db125e0e3c74c1dadbb32edae742411e28763ce2116dfd2e8202f", "start_char": 23464, "end_char": 24197, "text_sha256": "442fa593fda3c65b9c6391a3030401fd13548679459d4ccd58ea4da88d9fdfc6"}
experimental_model
MolyProbe live-cell FRET, MFSD5 overexpression and siRNA
exposure
Molybdate dose/time courses; 10 mM oxalate and 1 mM sulfate comparisons
limitations
The text reports millimolar values in this passage that differ from micromolar labeling elsewhere; this claim preserves the directional finding without inferring an exact effective concentration.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
Making much more of the transporter increased uptake in this cell model.
primary_references
[mo-p23472155] Exploring dynamics of molybdate in living animal cells by a genetically encoded FRET nanosensor. (2013). https://pubmed.ncbi.nlm.nih.gov/23472155/ DOI: 10.1371/journal.pone.0058175
tissue_or_cell_type
HEK-293T cells
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 222–233
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · MolyProbe live-cell FRET, MFSD5 overexpression and siRNA · source_derived_draft · unverified_draft
### mo-mfsd5-overexpression Large HsMOT2/MFSD5 overexpression increased the molybdate-sensitive FRET signal in HEK-293T cells. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Making much more of the transporter increased uptake in this cell model. organism: Homo sapiens tissue_or_cell_type: HEK-293T cells experimental_model: MolyProbe live-cell FRET, MFSD5 overexpression and siRNA limitations: The text reports millimolar values in this passage that differ from micromolar labeling elsewhere; this claim preserves the directional finding without inferring an exact effective concentration. exposure: Molybdate dose/time courses; 10 mM oxalate and 1 mM sulfate comparisons evidence_span: {"source_cache": "artifacts/molybdenum-research/23472155.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a3c76154f22db125e0e3c74c1dadbb32edae742411e28763ce2116dfd2e8202f", "start_char": 23464, "end_char": 24197, "text_sha256": "442fa593fda3c65b9c6391a3030401fd13548679459d4ccd58ea4da88d9fdfc6"} [mo-p23472155] Exploring dynamics of molybdate in living animal cells by a genetically encoded FRET nanosensor. (2013). https://pubmed.ncbi.nlm.nih.gov/23472155/ DOI: 10.1371/journal.pone.0058175
Complete structured claim and evidence
Reducing MFSD5 mRNA to 11-35% of control did not reduce molybdate uptake signals at the tested doses.
Human MFSD5 / HsMOT2 → Cellular molybdate uptake source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/23472155.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a3c76154f22db125e0e3c74c1dadbb32edae742411e28763ce2116dfd2e8202f", "start_char": 23464, "end_char": 24197, "text_sha256": "442fa593fda3c65b9c6391a3030401fd13548679459d4ccd58ea4da88d9fdfc6"}
experimental_model
MolyProbe live-cell FRET, MFSD5 overexpression and siRNA
exposure
Molybdate dose/time courses; 10 mM oxalate and 1 mM sulfate comparisons
limitations
FRET reports accessible molybdate, not total cofactor occupancy; mRNA knockdown does not prove complete protein depletion.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
This protein was not required for most measured uptake under these conditions.
primary_references
[mo-p23472155] Exploring dynamics of molybdate in living animal cells by a genetically encoded FRET nanosensor. (2013). https://pubmed.ncbi.nlm.nih.gov/23472155/ DOI: 10.1371/journal.pone.0058175
tissue_or_cell_type
HEK-293T cells
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 235–246
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · MolyProbe live-cell FRET, MFSD5 overexpression and siRNA · source_derived_draft · unverified_draft
### mo-mfsd5-knockdown-null Reducing MFSD5 mRNA to 11-35% of control did not reduce molybdate uptake signals at the tested doses. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: This protein was not required for most measured uptake under these conditions. organism: Homo sapiens tissue_or_cell_type: HEK-293T cells experimental_model: MolyProbe live-cell FRET, MFSD5 overexpression and siRNA limitations: FRET reports accessible molybdate, not total cofactor occupancy; mRNA knockdown does not prove complete protein depletion. exposure: Molybdate dose/time courses; 10 mM oxalate and 1 mM sulfate comparisons evidence_span: {"source_cache": "artifacts/molybdenum-research/23472155.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a3c76154f22db125e0e3c74c1dadbb32edae742411e28763ce2116dfd2e8202f", "start_char": 23464, "end_char": 24197, "text_sha256": "442fa593fda3c65b9c6391a3030401fd13548679459d4ccd58ea4da88d9fdfc6"} [mo-p23472155] Exploring dynamics of molybdate in living animal cells by a genetically encoded FRET nanosensor. (2013). https://pubmed.ncbi.nlm.nih.gov/23472155/ DOI: 10.1371/journal.pone.0058175
Complete structured claim and evidence
Oxalate at 10 mM inhibited molybdate accumulation in HEK-293T cells.
Oxalate → Cellular molybdate uptake source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/23472155.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a3c76154f22db125e0e3c74c1dadbb32edae742411e28763ce2116dfd2e8202f", "start_char": 21554, "end_char": 22593, "text_sha256": "79bbaf42eff93e67e445d38383c53bbd3cea5b18c2e2afee38803b40f9b5fc4c"}
experimental_model
MolyProbe live-cell FRET, MFSD5 overexpression and siRNA
exposure
Molybdate dose/time courses; 10 mM oxalate and 1 mM sulfate comparisons
limitations
High experimental concentration; does not establish dietary oxalate causing human molybdenum deficiency.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
High oxalate inhibited entry in this laboratory assay.
primary_references
[mo-p23472155] Exploring dynamics of molybdate in living animal cells by a genetically encoded FRET nanosensor. (2013). https://pubmed.ncbi.nlm.nih.gov/23472155/ DOI: 10.1371/journal.pone.0058175
tissue_or_cell_type
HEK-293T cells
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 248–259
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · MolyProbe live-cell FRET, MFSD5 overexpression and siRNA · source_derived_draft · unverified_draft
### mo-oxalate-uptake Oxalate at 10 mM inhibited molybdate accumulation in HEK-293T cells. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: High oxalate inhibited entry in this laboratory assay. organism: Homo sapiens tissue_or_cell_type: HEK-293T cells experimental_model: MolyProbe live-cell FRET, MFSD5 overexpression and siRNA limitations: High experimental concentration; does not establish dietary oxalate causing human molybdenum deficiency. exposure: Molybdate dose/time courses; 10 mM oxalate and 1 mM sulfate comparisons evidence_span: {"source_cache": "artifacts/molybdenum-research/23472155.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a3c76154f22db125e0e3c74c1dadbb32edae742411e28763ce2116dfd2e8202f", "start_char": 21554, "end_char": 22593, "text_sha256": "79bbaf42eff93e67e445d38383c53bbd3cea5b18c2e2afee38803b40f9b5fc4c"} [mo-p23472155] Exploring dynamics of molybdate in living animal cells by a genetically encoded FRET nanosensor. (2013). https://pubmed.ncbi.nlm.nih.gov/23472155/ DOI: 10.1371/journal.pone.0058175
Complete structured claim and evidence
Adding 1 mM sulfate had little effect on HEK-293T molybdate uptake signals.
Sulfate / SO4(2-) → Cellular molybdate uptake source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/23472155.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a3c76154f22db125e0e3c74c1dadbb32edae742411e28763ce2116dfd2e8202f", "start_char": 21554, "end_char": 22593, "text_sha256": "79bbaf42eff93e67e445d38383c53bbd3cea5b18c2e2afee38803b40f9b5fc4c"}
experimental_model
MolyProbe live-cell FRET, MFSD5 overexpression and siRNA
exposure
Molybdate dose/time courses; 10 mM oxalate and 1 mM sulfate comparisons
limitations
FRET reports accessible molybdate, not total cofactor occupancy; mRNA knockdown does not prove complete protein depletion.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
Sulfate did not strongly block this uptake route.
primary_references
[mo-p23472155] Exploring dynamics of molybdate in living animal cells by a genetically encoded FRET nanosensor. (2013). https://pubmed.ncbi.nlm.nih.gov/23472155/ DOI: 10.1371/journal.pone.0058175
tissue_or_cell_type
HEK-293T cells
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 261–272
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · MolyProbe live-cell FRET, MFSD5 overexpression and siRNA · source_derived_draft · unverified_draft
### mo-sulfate-uptake-null Adding 1 mM sulfate had little effect on HEK-293T molybdate uptake signals. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Sulfate did not strongly block this uptake route. organism: Homo sapiens tissue_or_cell_type: HEK-293T cells experimental_model: MolyProbe live-cell FRET, MFSD5 overexpression and siRNA limitations: FRET reports accessible molybdate, not total cofactor occupancy; mRNA knockdown does not prove complete protein depletion. exposure: Molybdate dose/time courses; 10 mM oxalate and 1 mM sulfate comparisons evidence_span: {"source_cache": "artifacts/molybdenum-research/23472155.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a3c76154f22db125e0e3c74c1dadbb32edae742411e28763ce2116dfd2e8202f", "start_char": 21554, "end_char": 22593, "text_sha256": "79bbaf42eff93e67e445d38383c53bbd3cea5b18c2e2afee38803b40f9b5fc4c"} [mo-p23472155] Exploring dynamics of molybdate in living animal cells by a genetically encoded FRET nanosensor. (2013). https://pubmed.ncbi.nlm.nih.gov/23472155/ DOI: 10.1371/journal.pone.0058175
Complete structured claim and evidence
Exon 1a targeted type I MOCS1A to the mitochondrial matrix, whereas exon 1b variants remained cytosolic.
Human molybdenum cofactor synthesis protein MOCS1A → Human MOCS1A-MOCS1B cPMP synthesis system source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/31996372.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a88a2e2c4aae83293fa6f1860d10bb41b41c32d1ad79b0b04cd5dd3eb02865c7", "start_char": 0, "end_char": 1846, "text_sha256": "a88a2e2c4aae83293fa6f1860d10bb41b41c32d1ad79b0b04cd5dd3eb02865c7"}
experimental_model
Alternative splicing, fluorescence microscopy, fractionation and mitochondrial targeting of human MOCS1 proteins
exposure
Type I-III MOCS1 splice constructs
limitations
Localization and processing experiments; no dietary iron, SAM or molybdenum intervention.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
Splicing changes where the first assembly protein goes.
primary_references
[mo-p31996372] Alternative splicing of the bicistronic gene molybdenum cofactor synthesis 1 (MOCS1) uncovers a novel mitochondrial protein maturation mechanism. (2020). https://pubmed.ncbi.nlm.nih.gov/31996372/ DOI: 10.1074/jbc.ra119.010720
tissue_or_cell_type
Transfected human-cell localization and mitochondrial matrix
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 287–298
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Alternative splicing, fluorescence microscopy, fractionation and mitochondrial targeting of human MOCS1 proteins · source_derived_draft · unverified_draft
### mo-mocs1a-targeting Exon 1a targeted type I MOCS1A to the mitochondrial matrix, whereas exon 1b variants remained cytosolic. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Splicing changes where the first assembly protein goes. organism: Homo sapiens tissue_or_cell_type: Transfected human-cell localization and mitochondrial matrix experimental_model: Alternative splicing, fluorescence microscopy, fractionation and mitochondrial targeting of human MOCS1 proteins limitations: Localization and processing experiments; no dietary iron, SAM or molybdenum intervention. exposure: Type I-III MOCS1 splice constructs evidence_span: {"source_cache": "artifacts/molybdenum-research/31996372.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a88a2e2c4aae83293fa6f1860d10bb41b41c32d1ad79b0b04cd5dd3eb02865c7", "start_char": 0, "end_char": 1846, "text_sha256": "a88a2e2c4aae83293fa6f1860d10bb41b41c32d1ad79b0b04cd5dd3eb02865c7"} [mo-p31996372] Alternative splicing of the bicistronic gene molybdenum cofactor synthesis 1 (MOCS1) uncovers a novel mitochondrial protein maturation mechanism. (2020). https://pubmed.ncbi.nlm.nih.gov/31996372/ DOI: 10.1074/jbc.ra119.010720
Complete structured claim and evidence
MOCS1AB fusion precursors underwent mitochondrial import and proteolytic cleavage that released the matrix-localized MOCS1B domain.
Human MOCS1AB fusion precursor → Human molybdenum cofactor synthesis protein MOCS1B source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/31996372.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a88a2e2c4aae83293fa6f1860d10bb41b41c32d1ad79b0b04cd5dd3eb02865c7", "start_char": 0, "end_char": 1846, "text_sha256": "a88a2e2c4aae83293fa6f1860d10bb41b41c32d1ad79b0b04cd5dd3eb02865c7"}
experimental_model
Alternative splicing, fluorescence microscopy, fractionation and mitochondrial targeting of human MOCS1 proteins
exposure
Type I-III MOCS1 splice constructs
limitations
Localization and processing experiments; no dietary iron, SAM or molybdenum intervention.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
A precursor protein must be imported and cut to release MOCS1B.
primary_references
[mo-p31996372] Alternative splicing of the bicistronic gene molybdenum cofactor synthesis 1 (MOCS1) uncovers a novel mitochondrial protein maturation mechanism. (2020). https://pubmed.ncbi.nlm.nih.gov/31996372/ DOI: 10.1074/jbc.ra119.010720
tissue_or_cell_type
Transfected human-cell localization and mitochondrial matrix
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 300–311
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Alternative splicing, fluorescence microscopy, fractionation and mitochondrial targeting of human MOCS1 proteins · source_derived_draft · unverified_draft
### mo-mocs1b-processing MOCS1AB fusion precursors underwent mitochondrial import and proteolytic cleavage that released the matrix-localized MOCS1B domain. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: A precursor protein must be imported and cut to release MOCS1B. organism: Homo sapiens tissue_or_cell_type: Transfected human-cell localization and mitochondrial matrix experimental_model: Alternative splicing, fluorescence microscopy, fractionation and mitochondrial targeting of human MOCS1 proteins limitations: Localization and processing experiments; no dietary iron, SAM or molybdenum intervention. exposure: Type I-III MOCS1 splice constructs evidence_span: {"source_cache": "artifacts/molybdenum-research/31996372.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a88a2e2c4aae83293fa6f1860d10bb41b41c32d1ad79b0b04cd5dd3eb02865c7", "start_char": 0, "end_char": 1846, "text_sha256": "a88a2e2c4aae83293fa6f1860d10bb41b41c32d1ad79b0b04cd5dd3eb02865c7"} [mo-p31996372] Alternative splicing of the bicistronic gene molybdenum cofactor synthesis 1 (MOCS1) uncovers a novel mitochondrial protein maturation mechanism. (2020). https://pubmed.ncbi.nlm.nih.gov/31996372/ DOI: 10.1074/jbc.ra119.010720
Complete structured claim and evidence
Anaerobic reconstitution yielded human MOCS1A containing two [4Fe-4S] clusters.
[4Fe-4S] iron-sulfur cluster → Human molybdenum cofactor synthesis protein MOCS1A source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/15180982.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "722c11f1c29a720fb7105f37962af2652ce95b6734afdb59d675dee0b8302097", "start_char": 0, "end_char": 1828, "text_sha256": "722c11f1c29a720fb7105f37962af2652ce95b6734afdb59d675dee0b8302097"}
experimental_model
Recombinant human MOCS1A, cysteine mutagenesis and multiple spectroscopic methods
exposure
Aerobic versus anaerobic purification; iron-sulfur reconstitution
limitations
Cluster states depend on preparation and oxygen exposure; the paper does not demonstrate a dietary iron or methyl-donor threshold.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Human protein expressed in Escherichia coli
plain_language
Molybdenum-cofactor assembly itself requires iron-sulfur machinery.
primary_references
[mo-p15180982] Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis. (2004). https://pubmed.ncbi.nlm.nih.gov/15180982/ DOI: 10.1074/jbc.m313398200
tissue_or_cell_type
Purified protein and bacterial complementation
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 313–324
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human MOCS1A, cysteine mutagenesis and multiple spectroscopic methods · source_derived_draft · unverified_draft
### mo-mocs1a-fes Anaerobic reconstitution yielded human MOCS1A containing two [4Fe-4S] clusters. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Molybdenum-cofactor assembly itself requires iron-sulfur machinery. organism: Human protein expressed in Escherichia coli tissue_or_cell_type: Purified protein and bacterial complementation experimental_model: Recombinant human MOCS1A, cysteine mutagenesis and multiple spectroscopic methods limitations: Cluster states depend on preparation and oxygen exposure; the paper does not demonstrate a dietary iron or methyl-donor threshold. exposure: Aerobic versus anaerobic purification; iron-sulfur reconstitution evidence_span: {"source_cache": "artifacts/molybdenum-research/15180982.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "722c11f1c29a720fb7105f37962af2652ce95b6734afdb59d675dee0b8302097", "start_char": 0, "end_char": 1828, "text_sha256": "722c11f1c29a720fb7105f37962af2652ce95b6734afdb59d675dee0b8302097"} [mo-p15180982] Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis. (2004). https://pubmed.ncbi.nlm.nih.gov/15180982/ DOI: 10.1074/jbc.m313398200
Complete structured claim and evidence
MOCS1A contains a redox-active N-terminal [4Fe-4S] cluster coordinated by the conserved radical-SAM cysteine motif.
Human molybdenum cofactor synthesis protein MOCS1A → S-Adenosyl-L-methionine source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/15180982.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "722c11f1c29a720fb7105f37962af2652ce95b6734afdb59d675dee0b8302097", "start_char": 0, "end_char": 1828, "text_sha256": "722c11f1c29a720fb7105f37962af2652ce95b6734afdb59d675dee0b8302097"}
experimental_model
Recombinant human MOCS1A, cysteine mutagenesis and multiple spectroscopic methods
exposure
Aerobic versus anaerobic purification; iron-sulfur reconstitution
limitations
The human protein study characterized clusters and essential cysteines; no human methylation-cycle depletion or clinical SAM requirement was measured.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Human protein expressed in Escherichia coli
plain_language
SAM participates in radical chemistry here; this is a different use from donating a methyl group to DNA.
primary_references
[mo-p15180982] Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis. (2004). https://pubmed.ncbi.nlm.nih.gov/15180982/ DOI: 10.1074/jbc.m313398200
tissue_or_cell_type
Purified protein and bacterial complementation
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 326–337
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human MOCS1A, cysteine mutagenesis and multiple spectroscopic methods · source_derived_draft · unverified_draft
### mo-mocs1a-radical-sam MOCS1A contains a redox-active N-terminal [4Fe-4S] cluster coordinated by the conserved radical-SAM cysteine motif. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: SAM participates in radical chemistry here; this is a different use from donating a methyl group to DNA. organism: Human protein expressed in Escherichia coli tissue_or_cell_type: Purified protein and bacterial complementation experimental_model: Recombinant human MOCS1A, cysteine mutagenesis and multiple spectroscopic methods limitations: The human protein study characterized clusters and essential cysteines; no human methylation-cycle depletion or clinical SAM requirement was measured. exposure: Aerobic versus anaerobic purification; iron-sulfur reconstitution evidence_span: {"source_cache": "artifacts/molybdenum-research/15180982.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "722c11f1c29a720fb7105f37962af2652ce95b6734afdb59d675dee0b8302097", "start_char": 0, "end_char": 1828, "text_sha256": "722c11f1c29a720fb7105f37962af2652ce95b6734afdb59d675dee0b8302097"} [mo-p15180982] Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis. (2004). https://pubmed.ncbi.nlm.nih.gov/15180982/ DOI: 10.1074/jbc.m313398200
Complete structured claim and evidence
Oxygen rapidly degraded both reconstituted MOCS1A [4Fe-4S] clusters, producing different semistable cluster intermediates.
Molecular oxygen → Human molybdenum cofactor synthesis protein MOCS1A source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/15180982.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "722c11f1c29a720fb7105f37962af2652ce95b6734afdb59d675dee0b8302097", "start_char": 0, "end_char": 1828, "text_sha256": "722c11f1c29a720fb7105f37962af2652ce95b6734afdb59d675dee0b8302097"}
experimental_model
Recombinant human MOCS1A, cysteine mutagenesis and multiple spectroscopic methods
exposure
Aerobic versus anaerobic purification; iron-sulfur reconstitution
limitations
Purified protein exposure; not evidence that normal breathing causes cofactor deficiency.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Human protein expressed in Escherichia coli
plain_language
The assembly protein contains oxygen-sensitive clusters.
primary_references
[mo-p15180982] Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis. (2004). https://pubmed.ncbi.nlm.nih.gov/15180982/ DOI: 10.1074/jbc.m313398200
tissue_or_cell_type
Purified protein and bacterial complementation
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 339–350
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human MOCS1A, cysteine mutagenesis and multiple spectroscopic methods · source_derived_draft · unverified_draft
### mo-mocs1a-oxygen Oxygen rapidly degraded both reconstituted MOCS1A [4Fe-4S] clusters, producing different semistable cluster intermediates. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The assembly protein contains oxygen-sensitive clusters. organism: Human protein expressed in Escherichia coli tissue_or_cell_type: Purified protein and bacterial complementation experimental_model: Recombinant human MOCS1A, cysteine mutagenesis and multiple spectroscopic methods limitations: Purified protein exposure; not evidence that normal breathing causes cofactor deficiency. exposure: Aerobic versus anaerobic purification; iron-sulfur reconstitution evidence_span: {"source_cache": "artifacts/molybdenum-research/15180982.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "722c11f1c29a720fb7105f37962af2652ce95b6734afdb59d675dee0b8302097", "start_char": 0, "end_char": 1828, "text_sha256": "722c11f1c29a720fb7105f37962af2652ce95b6734afdb59d675dee0b8302097"} [mo-p15180982] Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis. (2004). https://pubmed.ncbi.nlm.nih.gov/15180982/ DOI: 10.1074/jbc.m313398200
Complete structured claim and evidence
Purified NFS1 interacted specifically with MOCS3-RLD and supported sulfur transfer to it.
Human NFS1 sulfur-loaded persulfide state → Human adenylyltransferase and sulfurtransferase / MOCS3 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/18650437.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8180bd148722e8980ef5acbd4ae4c29a0d9d13da56bbccb91165a5eed4ab6f50", "start_char": 0, "end_char": 1547, "text_sha256": "8180bd148722e8980ef5acbd4ae4c29a0d9d13da56bbccb91165a5eed4ab6f50"}
experimental_model
Purified human NFS1/ISD11 and MOCS3 rhodanese-domain interaction and sulfur-transfer assays
exposure
L-cysteine sulfur-donor assays
limitations
Truncated and heterologously expressed proteins; cell localization was investigated independently in 2013.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Human proteins expressed in Escherichia coli
plain_language
The sulfur handoff uses identifiable proteins, not a free-floating mineral pool.
primary_references
[mo-p18650437] A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis. (2008). https://pubmed.ncbi.nlm.nih.gov/18650437/ DOI: 10.1074/jbc.m804064200
tissue_or_cell_type
Purified proteins
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 365–376
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human NFS1/ISD11 and MOCS3 rhodanese-domain interaction and sulfur-transfer assays · source_derived_draft · unverified_draft
### mo-nfs1-mocs3-transfer Purified NFS1 interacted specifically with MOCS3-RLD and supported sulfur transfer to it. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The sulfur handoff uses identifiable proteins, not a free-floating mineral pool. organism: Human proteins expressed in Escherichia coli tissue_or_cell_type: Purified proteins experimental_model: Purified human NFS1/ISD11 and MOCS3 rhodanese-domain interaction and sulfur-transfer assays limitations: Truncated and heterologously expressed proteins; cell localization was investigated independently in 2013. exposure: L-cysteine sulfur-donor assays evidence_span: {"source_cache": "artifacts/molybdenum-research/18650437.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8180bd148722e8980ef5acbd4ae4c29a0d9d13da56bbccb91165a5eed4ab6f50", "start_char": 0, "end_char": 1547, "text_sha256": "8180bd148722e8980ef5acbd4ae4c29a0d9d13da56bbccb91165a5eed4ab6f50"} [mo-p18650437] A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis. (2008). https://pubmed.ncbi.nlm.nih.gov/18650437/ DOI: 10.1074/jbc.m804064200
Complete structured claim and evidence
FRET and split-EGFP supported an NFS1-MOCS3 interaction in the cytosol of human cells.
Human cysteine desulfurase / NFS1 → Human adenylyltransferase and sulfurtransferase / MOCS3 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/23593335.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "de38fd3acf5b473459161bd9fc6bde8a7d13d8734336d445f36938684e50711b", "start_char": 0, "end_char": 1050, "text_sha256": "de38fd3acf5b473459161bd9fc6bde8a7d13d8734336d445f36938684e50711b"}
experimental_model
HeLa localization/FRET and split-EGFP; purified protein complementation
exposure
Cell fractionation, immunodetection and protein interaction
limitations
Cytosolic NFS1 is distinct from assuming all NFS1 sulfur transfer happens inside mitochondria.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens; separate Neurospora crassa complementation
plain_language
Sulfur delivery to the molybdenum pathway also occurs outside mitochondria.
primary_references
[mo-p23593335] The L-cysteine desulfurase NFS1 is localized in the cytosol where it provides the sulfur for molybdenum cofactor biosynthesis in humans. (2013). https://pubmed.ncbi.nlm.nih.gov/23593335/ DOI: 10.1371/journal.pone.0060869
tissue_or_cell_type
Human cytosol and purified proteins
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 378–389
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · HeLa localization/FRET and split-EGFP; purified protein complementation · source_derived_draft · unverified_draft
### mo-nfs1-cytosol FRET and split-EGFP supported an NFS1-MOCS3 interaction in the cytosol of human cells. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Sulfur delivery to the molybdenum pathway also occurs outside mitochondria. organism: Homo sapiens; separate Neurospora crassa complementation tissue_or_cell_type: Human cytosol and purified proteins experimental_model: HeLa localization/FRET and split-EGFP; purified protein complementation limitations: Cytosolic NFS1 is distinct from assuming all NFS1 sulfur transfer happens inside mitochondria. exposure: Cell fractionation, immunodetection and protein interaction evidence_span: {"source_cache": "artifacts/molybdenum-research/23593335.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "de38fd3acf5b473459161bd9fc6bde8a7d13d8734336d445f36938684e50711b", "start_char": 0, "end_char": 1050, "text_sha256": "de38fd3acf5b473459161bd9fc6bde8a7d13d8734336d445f36938684e50711b"} [mo-p23593335] The L-cysteine desulfurase NFS1 is localized in the cytosol where it provides the sulfur for molybdenum cofactor biosynthesis in humans. (2013). https://pubmed.ncbi.nlm.nih.gov/23593335/ DOI: 10.1371/journal.pone.0060869
Complete structured claim and evidence
The sulfur used to form the MPT dithiolene group is supplied from the C-terminal thiocarboxylate of the small MPT-synthase subunit.
Human MOCS2A C-terminal thiocarboxylate → Metal-free molybdopterin / MPT source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/12732628.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319", "start_char": 0, "end_char": 1322, "text_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319"}
experimental_model
Purified human MPT synthase and patient-derived point mutants
exposure
Precursor Z/cPMP conversion assays
limitations
In-vitro assembly and kinetic defects; severity comparisons refer to specific patients, not a universal hierarchy.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Human proteins expressed in Escherichia coli
plain_language
MOCS2A carries a chemically attached sulfur supply.
primary_references
[mo-p12732628] Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. (2003). https://pubmed.ncbi.nlm.nih.gov/12732628/ DOI: 10.1074/jbc.m303092200
tissue_or_cell_type
Reconstituted MOCS2A/MOCS2B tetramers
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 404–415
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human MPT synthase and patient-derived point mutants · source_derived_draft · unverified_draft
### mo-mocs2a-sulfur The sulfur used to form the MPT dithiolene group is supplied from the C-terminal thiocarboxylate of the small MPT-synthase subunit. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: MOCS2A carries a chemically attached sulfur supply. organism: Human proteins expressed in Escherichia coli tissue_or_cell_type: Reconstituted MOCS2A/MOCS2B tetramers experimental_model: Purified human MPT synthase and patient-derived point mutants limitations: In-vitro assembly and kinetic defects; severity comparisons refer to specific patients, not a universal hierarchy. exposure: Precursor Z/cPMP conversion assays evidence_span: {"source_cache": "artifacts/molybdenum-research/12732628.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319", "start_char": 0, "end_char": 1322, "text_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319"} [mo-p12732628] Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. (2003). https://pubmed.ncbi.nlm.nih.gov/12732628/ DOI: 10.1074/jbc.m303092200
Complete structured claim and evidence
MOCS2A Val7Phe weakened its interaction with MOCS2B in reconstituted human MPT synthase.
Human MOCS2A p.Val7Phe → Human molybdopterin synthase catalytic subunit / MOCS2B source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/12732628.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319", "start_char": 0, "end_char": 1322, "text_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319"}
experimental_model
Purified human MPT synthase and patient-derived point mutants
exposure
Precursor Z/cPMP conversion assays
limitations
In-vitro assembly and kinetic defects; severity comparisons refer to specific patients, not a universal hierarchy.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Human proteins expressed in Escherichia coli
plain_language
A damaged sulfur-carrier subunit may no longer fit its partner.
primary_references
[mo-p12732628] Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. (2003). https://pubmed.ncbi.nlm.nih.gov/12732628/ DOI: 10.1074/jbc.m303092200
tissue_or_cell_type
Reconstituted MOCS2A/MOCS2B tetramers
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 417–428
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human MPT synthase and patient-derived point mutants · source_derived_draft · unverified_draft
### mo-mocs2a-v7f MOCS2A Val7Phe weakened its interaction with MOCS2B in reconstituted human MPT synthase. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: A damaged sulfur-carrier subunit may no longer fit its partner. organism: Human proteins expressed in Escherichia coli tissue_or_cell_type: Reconstituted MOCS2A/MOCS2B tetramers experimental_model: Purified human MPT synthase and patient-derived point mutants limitations: In-vitro assembly and kinetic defects; severity comparisons refer to specific patients, not a universal hierarchy. exposure: Precursor Z/cPMP conversion assays evidence_span: {"source_cache": "artifacts/molybdenum-research/12732628.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319", "start_char": 0, "end_char": 1322, "text_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319"} [mo-p12732628] Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. (2003). https://pubmed.ncbi.nlm.nih.gov/12732628/ DOI: 10.1074/jbc.m303092200
Complete structured claim and evidence
MOCS2B Glu168Lys attenuated binding of precursor Z/cPMP.
Human MOCS2B p.Glu168Lys → Cyclic pyranopterin monophosphate / cPMP source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/12732628.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319", "start_char": 0, "end_char": 1322, "text_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319"}
experimental_model
Purified human MPT synthase and patient-derived point mutants
exposure
Precursor Z/cPMP conversion assays
limitations
In-vitro assembly and kinetic defects; severity comparisons refer to specific patients, not a universal hierarchy.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Human proteins expressed in Escherichia coli
plain_language
A different mutation disrupts capture of the precursor.
primary_references
[mo-p12732628] Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. (2003). https://pubmed.ncbi.nlm.nih.gov/12732628/ DOI: 10.1074/jbc.m303092200
tissue_or_cell_type
Reconstituted MOCS2A/MOCS2B tetramers
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 430–441
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human MPT synthase and patient-derived point mutants · source_derived_draft · unverified_draft
### mo-mocs2b-e168k MOCS2B Glu168Lys attenuated binding of precursor Z/cPMP. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: A different mutation disrupts capture of the precursor. organism: Human proteins expressed in Escherichia coli tissue_or_cell_type: Reconstituted MOCS2A/MOCS2B tetramers experimental_model: Purified human MPT synthase and patient-derived point mutants limitations: In-vitro assembly and kinetic defects; severity comparisons refer to specific patients, not a universal hierarchy. exposure: Precursor Z/cPMP conversion assays evidence_span: {"source_cache": "artifacts/molybdenum-research/12732628.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319", "start_char": 0, "end_char": 1322, "text_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319"} [mo-p12732628] Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. (2003). https://pubmed.ncbi.nlm.nih.gov/12732628/ DOI: 10.1074/jbc.m303092200
Complete structured claim and evidence
MOCS3 also activates URM1 by adenylation and sulfur transfer to its terminal glycine.
Human adenylyltransferase and sulfurtransferase / MOCS3 → Human ubiquitin-related modifier / URM1 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/22453920.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "700833295a22a72be9d0ee74144bfe9249d6266c7fcba7b48330a4b2f2bf9c64", "start_char": 0, "end_char": 1267, "text_sha256": "700833295a22a72be9d0ee74144bfe9249d6266c7fcba7b48330a4b2f2bf9c64"}
experimental_model
Human-cell interaction/localization and purified-protein adenylation/sulfuration
exposure
MOCS2A and URM1 terminal glycine variants
limitations
Shared enzyme does not prove competition for sulfur in ordinary nutrient deficiency.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
The same sulfur-handling enzyme supplies a separate RNA-modification pathway.
primary_references
[mo-p22453920] Dual role of the molybdenum cofactor biosynthesis protein MOCS3 in tRNA thiolation and molybdenum cofactor biosynthesis in humans. (2012). https://pubmed.ncbi.nlm.nih.gov/22453920/ DOI: 10.1074/jbc.m112.351429
tissue_or_cell_type
Cytosolic sulfur-transfer pathways
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 456–467
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human-cell interaction/localization and purified-protein adenylation/sulfuration · source_derived_draft · unverified_draft
### mo-mocs3-urm1 MOCS3 also activates URM1 by adenylation and sulfur transfer to its terminal glycine. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The same sulfur-handling enzyme supplies a separate RNA-modification pathway. organism: Homo sapiens tissue_or_cell_type: Cytosolic sulfur-transfer pathways experimental_model: Human-cell interaction/localization and purified-protein adenylation/sulfuration limitations: Shared enzyme does not prove competition for sulfur in ordinary nutrient deficiency. exposure: MOCS2A and URM1 terminal glycine variants evidence_span: {"source_cache": "artifacts/molybdenum-research/22453920.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "700833295a22a72be9d0ee74144bfe9249d6266c7fcba7b48330a4b2f2bf9c64", "start_char": 0, "end_char": 1267, "text_sha256": "700833295a22a72be9d0ee74144bfe9249d6266c7fcba7b48330a4b2f2bf9c64"} [mo-p22453920] Dual role of the molybdenum cofactor biosynthesis protein MOCS3 in tRNA thiolation and molybdenum cofactor biosynthesis in humans. (2012). https://pubmed.ncbi.nlm.nih.gov/22453920/ DOI: 10.1074/jbc.m112.351429
Complete structured claim and evidence
Removing the terminal glycine from MOCS2A or URM1 abolished the measured interaction with MOCS3.
Human molybdopterin synthase sulfur carrier / MOCS2A → Human adenylyltransferase and sulfurtransferase / MOCS3 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/22453920.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "700833295a22a72be9d0ee74144bfe9249d6266c7fcba7b48330a4b2f2bf9c64", "start_char": 0, "end_char": 1267, "text_sha256": "700833295a22a72be9d0ee74144bfe9249d6266c7fcba7b48330a4b2f2bf9c64"}
experimental_model
Human-cell interaction/localization and purified-protein adenylation/sulfuration
exposure
MOCS2A and URM1 terminal glycine variants
limitations
Shared enzyme does not prove competition for sulfur in ordinary nutrient deficiency.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
The sulfur handoff depends on the receiving protein having the right end.
primary_references
[mo-p22453920] Dual role of the molybdenum cofactor biosynthesis protein MOCS3 in tRNA thiolation and molybdenum cofactor biosynthesis in humans. (2012). https://pubmed.ncbi.nlm.nih.gov/22453920/ DOI: 10.1074/jbc.m112.351429
tissue_or_cell_type
Cytosolic sulfur-transfer pathways
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 469–480
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human-cell interaction/localization and purified-protein adenylation/sulfuration · source_derived_draft · unverified_draft
### mo-mocs3-terminal-glycine Removing the terminal glycine from MOCS2A or URM1 abolished the measured interaction with MOCS3. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The sulfur handoff depends on the receiving protein having the right end. organism: Homo sapiens tissue_or_cell_type: Cytosolic sulfur-transfer pathways experimental_model: Human-cell interaction/localization and purified-protein adenylation/sulfuration limitations: Shared enzyme does not prove competition for sulfur in ordinary nutrient deficiency. exposure: MOCS2A and URM1 terminal glycine variants evidence_span: {"source_cache": "artifacts/molybdenum-research/22453920.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "700833295a22a72be9d0ee74144bfe9249d6266c7fcba7b48330a4b2f2bf9c64", "start_char": 0, "end_char": 1267, "text_sha256": "700833295a22a72be9d0ee74144bfe9249d6266c7fcba7b48330a4b2f2bf9c64"} [mo-p22453920] Dual role of the molybdenum cofactor biosynthesis protein MOCS3 in tRNA thiolation and molybdenum cofactor biosynthesis in humans. (2012). https://pubmed.ncbi.nlm.nih.gov/22453920/ DOI: 10.1074/jbc.m112.351429
Complete structured claim and evidence
Full gephyrin supported over 300-fold greater Moco synthesis than the separated G and E domains in the reported reconstitution system.
Human gephyrin / GPHN → Molybdenum cofactor / Moco source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/23163752.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "909388cf5fb7bfa5d2f8444644e20773a7a8ec6a19b4ccb8a4bda78d9ad17c5d", "start_char": 0, "end_char": 1489, "text_sha256": "909388cf5fb7bfa5d2f8444644e20773a7a8ec6a19b4ccb8a4bda78d9ad17c5d"}
experimental_model
Purified mammalian gephyrin domains and full multidomain protein; in-vitro Moco reconstitution
exposure
MPT adenylation, molybdate insertion and domain-combination assays
limitations
No human dietary magnesium intervention; purified domain kinetics should not be turned into supplementation efficacy.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Mammalian protein system
plain_language
Keeping the two reactions together makes cofactor assembly much more efficient.
primary_references
[mo-p23163752] Metal insertion into the molybdenum cofactor: product-substrate channelling demonstrates the functional origin of domain fusion in gephyrin. (2013). https://pubmed.ncbi.nlm.nih.gov/23163752/ DOI: 10.1042/bj20121078
tissue_or_cell_type
Purified gephyrin
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 508–519
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified mammalian gephyrin domains and full multidomain protein; in-vitro Moco reconstitution · source_derived_draft · unverified_draft
### mo-gphn-channeling Full gephyrin supported over 300-fold greater Moco synthesis than the separated G and E domains in the reported reconstitution system. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Keeping the two reactions together makes cofactor assembly much more efficient. organism: Mammalian protein system tissue_or_cell_type: Purified gephyrin experimental_model: Purified mammalian gephyrin domains and full multidomain protein; in-vitro Moco reconstitution limitations: No human dietary magnesium intervention; purified domain kinetics should not be turned into supplementation efficacy. exposure: MPT adenylation, molybdate insertion and domain-combination assays evidence_span: {"source_cache": "artifacts/molybdenum-research/23163752.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "909388cf5fb7bfa5d2f8444644e20773a7a8ec6a19b4ccb8a4bda78d9ad17c5d", "start_char": 0, "end_char": 1489, "text_sha256": "909388cf5fb7bfa5d2f8444644e20773a7a8ec6a19b4ccb8a4bda78d9ad17c5d"} [mo-p23163752] Metal insertion into the molybdenum cofactor: product-substrate channelling demonstrates the functional origin of domain fusion in gephyrin. (2013). https://pubmed.ncbi.nlm.nih.gov/23163752/ DOI: 10.1042/bj20121078
Complete structured claim and evidence
The purified human MOCOS NifS-like domain bound PLP and exhibited cysteine desulfurase activity.
PLP → Human molybdenum cofactor sulfurase / MOCOS source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/34356852.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8bf3a09c4f88994cf8adc50faf391e62ac27e7572e59e6606147f2c689212d07", "start_char": 41304, "end_char": 42029, "text_sha256": "b9b02aae5eb537bdffc178ceaa33177cef6448738c19cb1a8477ad543f4e970c"}
experimental_model
Xanthinuria families with recombinant human MOCOS-domain assays and a plant XDH homolog assay
exposure
PLP quantification, cysteine desulfurase assays and Moco/MPT binding
limitations
Human XDH C150F was functionally modeled using Arabidopsis XDH1 C161S, not purified human C150F; MOCOS assays used isolated domains.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Human genetics and human MOCOS proteins; plant XDH variant experiment separately
plain_language
Vitamin B6 chemistry helps supply the sulfur used to activate these molybdenum enzymes.
primary_references
[mo-p34356852] Classical Xanthinuria in Nine Israeli Families and Two Isolated Cases from Germany: Molecular, Biochemical and Population Genetics Aspects. (2021). https://pubmed.ncbi.nlm.nih.gov/34356852/ DOI: 10.3390/biomedicines9070788
tissue_or_cell_type
Patient samples and purified domains
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 534–545
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Xanthinuria families with recombinant human MOCOS-domain assays and a plant XDH homolog assay · source_derived_draft · unverified_draft
### mo-mocos-plp The purified human MOCOS NifS-like domain bound PLP and exhibited cysteine desulfurase activity. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Vitamin B6 chemistry helps supply the sulfur used to activate these molybdenum enzymes. organism: Human genetics and human MOCOS proteins; plant XDH variant experiment separately tissue_or_cell_type: Patient samples and purified domains experimental_model: Xanthinuria families with recombinant human MOCOS-domain assays and a plant XDH homolog assay limitations: Human XDH C150F was functionally modeled using Arabidopsis XDH1 C161S, not purified human C150F; MOCOS assays used isolated domains. exposure: PLP quantification, cysteine desulfurase assays and Moco/MPT binding evidence_span: {"source_cache": "artifacts/molybdenum-research/34356852.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8bf3a09c4f88994cf8adc50faf391e62ac27e7572e59e6606147f2c689212d07", "start_char": 41304, "end_char": 42029, "text_sha256": "b9b02aae5eb537bdffc178ceaa33177cef6448738c19cb1a8477ad543f4e970c"} [mo-p34356852] Classical Xanthinuria in Nine Israeli Families and Two Isolated Cases from Germany: Molecular, Biochemical and Population Genetics Aspects. (2021). https://pubmed.ncbi.nlm.nih.gov/34356852/ DOI: 10.3390/biomedicines9070788
Complete structured claim and evidence
The Thr349Ile MOCOS N-terminal domain had severely impaired cysteine desulfurase activity, including a preparation with measurable PLP binding.
Human MOCOS p.Thr349Ile → Human molybdenum cofactor sulfurase / MOCOS source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/34356852.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8bf3a09c4f88994cf8adc50faf391e62ac27e7572e59e6606147f2c689212d07", "start_char": 41304, "end_char": 42029, "text_sha256": "b9b02aae5eb537bdffc178ceaa33177cef6448738c19cb1a8477ad543f4e970c"}
experimental_model
Xanthinuria families with recombinant human MOCOS-domain assays and a plant XDH homolog assay
exposure
PLP quantification, cysteine desulfurase assays and Moco/MPT binding
limitations
Human XDH C150F was functionally modeled using Arabidopsis XDH1 C161S, not purified human C150F; MOCOS assays used isolated domains.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Human genetics and human MOCOS proteins; plant XDH variant experiment separately
plain_language
Having some B6 cofactor bound did not repair the defective enzyme.
primary_references
[mo-p34356852] Classical Xanthinuria in Nine Israeli Families and Two Isolated Cases from Germany: Molecular, Biochemical and Population Genetics Aspects. (2021). https://pubmed.ncbi.nlm.nih.gov/34356852/ DOI: 10.3390/biomedicines9070788
tissue_or_cell_type
Patient samples and purified domains
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 547–558
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Xanthinuria families with recombinant human MOCOS-domain assays and a plant XDH homolog assay · source_derived_draft · unverified_draft
### mo-mocos-t349i The Thr349Ile MOCOS N-terminal domain had severely impaired cysteine desulfurase activity, including a preparation with measurable PLP binding. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Having some B6 cofactor bound did not repair the defective enzyme. organism: Human genetics and human MOCOS proteins; plant XDH variant experiment separately tissue_or_cell_type: Patient samples and purified domains experimental_model: Xanthinuria families with recombinant human MOCOS-domain assays and a plant XDH homolog assay limitations: Human XDH C150F was functionally modeled using Arabidopsis XDH1 C161S, not purified human C150F; MOCOS assays used isolated domains. exposure: PLP quantification, cysteine desulfurase assays and Moco/MPT binding evidence_span: {"source_cache": "artifacts/molybdenum-research/34356852.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8bf3a09c4f88994cf8adc50faf391e62ac27e7572e59e6606147f2c689212d07", "start_char": 41304, "end_char": 42029, "text_sha256": "b9b02aae5eb537bdffc178ceaa33177cef6448738c19cb1a8477ad543f4e970c"} [mo-p34356852] Classical Xanthinuria in Nine Israeli Families and Two Isolated Cases from Germany: Molecular, Biochemical and Population Genetics Aspects. (2021). https://pubmed.ncbi.nlm.nih.gov/34356852/ DOI: 10.3390/biomedicines9070788
Complete structured claim and evidence
MOCOS Pro591Ser impaired cofactor binding in the C-terminal domain assay.
Human MOCOS p.Pro591Ser → Molybdenum cofactor / Moco source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/34356852.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9a7e4ebde1063db92cef7c8b18753b2d2af12f8f132cad45fc2e3ae00b911f96", "start_char": 0, "end_char": 1697, "text_sha256": "9a7e4ebde1063db92cef7c8b18753b2d2af12f8f132cad45fc2e3ae00b911f96"}
experimental_model
Xanthinuria families with recombinant human MOCOS-domain assays and a plant XDH homolog assay
exposure
PLP quantification, cysteine desulfurase assays and Moco/MPT binding
limitations
Human XDH C150F was functionally modeled using Arabidopsis XDH1 C161S, not purified human C150F; MOCOS assays used isolated domains.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Human genetics and human MOCOS proteins; plant XDH variant experiment separately
plain_language
This variant disrupts the cofactor-binding side of the sulfurase.
primary_references
[mo-p34356852] Classical Xanthinuria in Nine Israeli Families and Two Isolated Cases from Germany: Molecular, Biochemical and Population Genetics Aspects. (2021). https://pubmed.ncbi.nlm.nih.gov/34356852/ DOI: 10.3390/biomedicines9070788
tissue_or_cell_type
Patient samples and purified domains
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 560–571
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Xanthinuria families with recombinant human MOCOS-domain assays and a plant XDH homolog assay · source_derived_draft · unverified_draft
### mo-mocos-p591s MOCOS Pro591Ser impaired cofactor binding in the C-terminal domain assay. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: This variant disrupts the cofactor-binding side of the sulfurase. organism: Human genetics and human MOCOS proteins; plant XDH variant experiment separately tissue_or_cell_type: Patient samples and purified domains experimental_model: Xanthinuria families with recombinant human MOCOS-domain assays and a plant XDH homolog assay limitations: Human XDH C150F was functionally modeled using Arabidopsis XDH1 C161S, not purified human C150F; MOCOS assays used isolated domains. exposure: PLP quantification, cysteine desulfurase assays and Moco/MPT binding evidence_span: {"source_cache": "artifacts/molybdenum-research/34356852.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9a7e4ebde1063db92cef7c8b18753b2d2af12f8f132cad45fc2e3ae00b911f96", "start_char": 0, "end_char": 1697, "text_sha256": "9a7e4ebde1063db92cef7c8b18753b2d2af12f8f132cad45fc2e3ae00b911f96"} [mo-p34356852] Classical Xanthinuria in Nine Israeli Families and Two Isolated Cases from Germany: Molecular, Biochemical and Population Genetics Aspects. (2021). https://pubmed.ncbi.nlm.nih.gov/34356852/ DOI: 10.3390/biomedicines9070788
Complete structured claim and evidence
MOCOS Arg776Cys impaired cofactor binding in the C-terminal domain assay.
Human MOCOS p.Arg776Cys → Molybdenum cofactor / Moco source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/34356852.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9a7e4ebde1063db92cef7c8b18753b2d2af12f8f132cad45fc2e3ae00b911f96", "start_char": 0, "end_char": 1697, "text_sha256": "9a7e4ebde1063db92cef7c8b18753b2d2af12f8f132cad45fc2e3ae00b911f96"}
experimental_model
Xanthinuria families with recombinant human MOCOS-domain assays and a plant XDH homolog assay
exposure
PLP quantification, cysteine desulfurase assays and Moco/MPT binding
limitations
Human XDH C150F was functionally modeled using Arabidopsis XDH1 C161S, not purified human C150F; MOCOS assays used isolated domains.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Human genetics and human MOCOS proteins; plant XDH variant experiment separately
plain_language
A second variant damages the same cofactor-handling stage.
primary_references
[mo-p34356852] Classical Xanthinuria in Nine Israeli Families and Two Isolated Cases from Germany: Molecular, Biochemical and Population Genetics Aspects. (2021). https://pubmed.ncbi.nlm.nih.gov/34356852/ DOI: 10.3390/biomedicines9070788
tissue_or_cell_type
Patient samples and purified domains
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 573–584
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Xanthinuria families with recombinant human MOCOS-domain assays and a plant XDH homolog assay · source_derived_draft · unverified_draft
### mo-mocos-r776c MOCOS Arg776Cys impaired cofactor binding in the C-terminal domain assay. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: A second variant damages the same cofactor-handling stage. organism: Human genetics and human MOCOS proteins; plant XDH variant experiment separately tissue_or_cell_type: Patient samples and purified domains experimental_model: Xanthinuria families with recombinant human MOCOS-domain assays and a plant XDH homolog assay limitations: Human XDH C150F was functionally modeled using Arabidopsis XDH1 C161S, not purified human C150F; MOCOS assays used isolated domains. exposure: PLP quantification, cysteine desulfurase assays and Moco/MPT binding evidence_span: {"source_cache": "artifacts/molybdenum-research/34356852.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9a7e4ebde1063db92cef7c8b18753b2d2af12f8f132cad45fc2e3ae00b911f96", "start_char": 0, "end_char": 1697, "text_sha256": "9a7e4ebde1063db92cef7c8b18753b2d2af12f8f132cad45fc2e3ae00b911f96"} [mo-p34356852] Classical Xanthinuria in Nine Israeli Families and Two Isolated Cases from Germany: Molecular, Biochemical and Population Genetics Aspects. (2021). https://pubmed.ncbi.nlm.nih.gov/34356852/ DOI: 10.3390/biomedicines9070788
Complete structured claim and evidence
SUOX sulfite oxidation depends on Moco at the catalytic site and a separate heme cofactor.
Molybdenum cofactor / Moco → Human sulfite oxidase / SUOX source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/31127934.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d0efd64e9cde371d0223d63607f5f6b76aada3a628c526f915d9b306c9bef7de", "start_char": 0, "end_char": 1649, "text_sha256": "d0efd64e9cde371d0223d63607f5f6b76aada3a628c526f915d9b306c9bef7de"}
experimental_model
Human SUOX Gly362Ser patient fibroblasts and recombinant enzyme maturation assays
exposure
G362S versus WT protein; Moco reconstitution and molybdate supplementation in culture
limitations
One genotype; in-vitro molybdate rescue is not demonstrated clinical treatment for all SUOX defects.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
Molybdenum and iron-containing heme perform different jobs within this enzyme.
primary_references
[mo-p31127934] Impaired mitochondrial maturation of sulfite oxidase in a patient with severe sulfite oxidase deficiency. (2019). https://pubmed.ncbi.nlm.nih.gov/31127934/ DOI: 10.1093/hmg/ddz109
tissue_or_cell_type
Mitochondrial intermembrane space; patient fibroblasts
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 599–610
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human SUOX Gly362Ser patient fibroblasts and recombinant enzyme maturation assays · source_derived_draft · unverified_draft
### mo-suox-cofactors SUOX sulfite oxidation depends on Moco at the catalytic site and a separate heme cofactor. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Molybdenum and iron-containing heme perform different jobs within this enzyme. organism: Homo sapiens tissue_or_cell_type: Mitochondrial intermembrane space; patient fibroblasts experimental_model: Human SUOX Gly362Ser patient fibroblasts and recombinant enzyme maturation assays limitations: One genotype; in-vitro molybdate rescue is not demonstrated clinical treatment for all SUOX defects. exposure: G362S versus WT protein; Moco reconstitution and molybdate supplementation in culture evidence_span: {"source_cache": "artifacts/molybdenum-research/31127934.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d0efd64e9cde371d0223d63607f5f6b76aada3a628c526f915d9b306c9bef7de", "start_char": 0, "end_char": 1649, "text_sha256": "d0efd64e9cde371d0223d63607f5f6b76aada3a628c526f915d9b306c9bef7de"} [mo-p31127934] Impaired mitochondrial maturation of sulfite oxidase in a patient with severe sulfite oxidase deficiency. (2019). https://pubmed.ncbi.nlm.nih.gov/31127934/ DOI: 10.1093/hmg/ddz109
Complete structured claim and evidence
Apo-G362S SUOX reconstituted with Moco about 90-fold less efficiently than wild type; patient fibroblasts had no detectable activity.
Human SUOX p.Gly362Ser → Molybdenum cofactor / Moco source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/31127934.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d0efd64e9cde371d0223d63607f5f6b76aada3a628c526f915d9b306c9bef7de", "start_char": 0, "end_char": 1649, "text_sha256": "d0efd64e9cde371d0223d63607f5f6b76aada3a628c526f915d9b306c9bef7de"}
experimental_model
Human SUOX Gly362Ser patient fibroblasts and recombinant enzyme maturation assays
exposure
G362S versus WT protein; Moco reconstitution and molybdate supplementation in culture
limitations
One genotype; in-vitro molybdate rescue is not demonstrated clinical treatment for all SUOX defects.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
The defect is in loading the cofactor, not simply in the amount of enzyme protein.
primary_references
[mo-p31127934] Impaired mitochondrial maturation of sulfite oxidase in a patient with severe sulfite oxidase deficiency. (2019). https://pubmed.ncbi.nlm.nih.gov/31127934/ DOI: 10.1093/hmg/ddz109
tissue_or_cell_type
Mitochondrial intermembrane space; patient fibroblasts
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 612–623
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human SUOX Gly362Ser patient fibroblasts and recombinant enzyme maturation assays · source_derived_draft · unverified_draft
### mo-suox-g362s-maturation Apo-G362S SUOX reconstituted with Moco about 90-fold less efficiently than wild type; patient fibroblasts had no detectable activity. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The defect is in loading the cofactor, not simply in the amount of enzyme protein. organism: Homo sapiens tissue_or_cell_type: Mitochondrial intermembrane space; patient fibroblasts experimental_model: Human SUOX Gly362Ser patient fibroblasts and recombinant enzyme maturation assays limitations: One genotype; in-vitro molybdate rescue is not demonstrated clinical treatment for all SUOX defects. exposure: G362S versus WT protein; Moco reconstitution and molybdate supplementation in culture evidence_span: {"source_cache": "artifacts/molybdenum-research/31127934.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d0efd64e9cde371d0223d63607f5f6b76aada3a628c526f915d9b306c9bef7de", "start_char": 0, "end_char": 1649, "text_sha256": "d0efd64e9cde371d0223d63607f5f6b76aada3a628c526f915d9b306c9bef7de"} [mo-p31127934] Impaired mitochondrial maturation of sulfite oxidase in a patient with severe sulfite oxidase deficiency. (2019). https://pubmed.ncbi.nlm.nih.gov/31127934/ DOI: 10.1093/hmg/ddz109
Complete structured claim and evidence
Adding molybdate to culture medium partially rescued Moco binding and restored detectable SUOX activity in the G362S patient fibroblasts.
Molybdate / MoO4(2-) → Human SUOX p.Gly362Ser source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/31127934.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d0efd64e9cde371d0223d63607f5f6b76aada3a628c526f915d9b306c9bef7de", "start_char": 0, "end_char": 1649, "text_sha256": "d0efd64e9cde371d0223d63607f5f6b76aada3a628c526f915d9b306c9bef7de"}
experimental_model
Human SUOX Gly362Ser patient fibroblasts and recombinant enzyme maturation assays
exposure
G362S versus WT protein; Moco reconstitution and molybdate supplementation in culture
limitations
Cell-culture rescue of one variant; no oral dose, clinical efficacy or universal rescue is established.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
Extra molybdate helped this particular cellular maturation defect.
primary_references
[mo-p31127934] Impaired mitochondrial maturation of sulfite oxidase in a patient with severe sulfite oxidase deficiency. (2019). https://pubmed.ncbi.nlm.nih.gov/31127934/ DOI: 10.1093/hmg/ddz109
tissue_or_cell_type
Mitochondrial intermembrane space; patient fibroblasts
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 625–636
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human SUOX Gly362Ser patient fibroblasts and recombinant enzyme maturation assays · source_derived_draft · unverified_draft
### mo-suox-g362s-rescue Adding molybdate to culture medium partially rescued Moco binding and restored detectable SUOX activity in the G362S patient fibroblasts. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Extra molybdate helped this particular cellular maturation defect. organism: Homo sapiens tissue_or_cell_type: Mitochondrial intermembrane space; patient fibroblasts experimental_model: Human SUOX Gly362Ser patient fibroblasts and recombinant enzyme maturation assays limitations: Cell-culture rescue of one variant; no oral dose, clinical efficacy or universal rescue is established. exposure: G362S versus WT protein; Moco reconstitution and molybdate supplementation in culture evidence_span: {"source_cache": "artifacts/molybdenum-research/31127934.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d0efd64e9cde371d0223d63607f5f6b76aada3a628c526f915d9b306c9bef7de", "start_char": 0, "end_char": 1649, "text_sha256": "d0efd64e9cde371d0223d63607f5f6b76aada3a628c526f915d9b306c9bef7de"} [mo-p31127934] Impaired mitochondrial maturation of sulfite oxidase in a patient with severe sulfite oxidase deficiency. (2019). https://pubmed.ncbi.nlm.nih.gov/31127934/ DOI: 10.1093/hmg/ddz109
Complete structured claim and evidence
Moco binding was required for mitochondrial trapping and retention of processed sulfite oxidase.
Molybdenum cofactor / Moco → Mitochondrial retention of sulfite oxidase source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/22854042.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "01970920183b87fde6830ca30d612aff75fc4b1a30672a3b9cc2f0c408294884", "start_char": 0, "end_char": 1268, "text_sha256": "01970920183b87fde6830ca30d612aff75fc4b1a30672a3b9cc2f0c408294884"}
experimental_model
Mammalian sulfite-oxidase targeting, cofactor depletion and maturation experiments
exposure
Targeting-sequence constructs and absence of Moco
limitations
Sequential maturation in the studied models; not a universal ranking of nutrient needs.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Mammalian/human cell models
plain_language
The cofactor helps keep SUOX in the compartment where it works.
primary_references
[mo-p22854042] Cofactor-dependent maturation of mammalian sulfite oxidase links two mitochondrial import pathways. (2012). https://pubmed.ncbi.nlm.nih.gov/22854042/ DOI: 10.1242/jcs.110114
tissue_or_cell_type
Mitochondrial intermembrane space and cytosol
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 638–649
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Mammalian sulfite-oxidase targeting, cofactor depletion and maturation experiments · source_derived_draft · unverified_draft
### mo-suox-moco-trap Moco binding was required for mitochondrial trapping and retention of processed sulfite oxidase. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The cofactor helps keep SUOX in the compartment where it works. organism: Mammalian/human cell models tissue_or_cell_type: Mitochondrial intermembrane space and cytosol experimental_model: Mammalian sulfite-oxidase targeting, cofactor depletion and maturation experiments limitations: Sequential maturation in the studied models; not a universal ranking of nutrient needs. exposure: Targeting-sequence constructs and absence of Moco evidence_span: {"source_cache": "artifacts/molybdenum-research/22854042.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "01970920183b87fde6830ca30d612aff75fc4b1a30672a3b9cc2f0c408294884", "start_char": 0, "end_char": 1268, "text_sha256": "01970920183b87fde6830ca30d612aff75fc4b1a30672a3b9cc2f0c408294884"} [mo-p22854042] Cofactor-dependent maturation of mammalian sulfite oxidase links two mitochondrial import pathways. (2012). https://pubmed.ncbi.nlm.nih.gov/22854042/ DOI: 10.1242/jcs.110114
Complete structured claim and evidence
Heme binding occurred only after Moco integration in the studied SUOX maturation pathway.
Molybdenum cofactor / Moco → Sulfite oxidase heme loading source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/22854042.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "01970920183b87fde6830ca30d612aff75fc4b1a30672a3b9cc2f0c408294884", "start_char": 0, "end_char": 1268, "text_sha256": "01970920183b87fde6830ca30d612aff75fc4b1a30672a3b9cc2f0c408294884"}
experimental_model
Mammalian sulfite-oxidase targeting, cofactor depletion and maturation experiments
exposure
Targeting-sequence constructs and absence of Moco
limitations
Sequential maturation in the studied models; not a universal ranking of nutrient needs.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Mammalian/human cell models
plain_language
Iron-containing heme is loaded after the molybdenum cofactor.
primary_references
[mo-p22854042] Cofactor-dependent maturation of mammalian sulfite oxidase links two mitochondrial import pathways. (2012). https://pubmed.ncbi.nlm.nih.gov/22854042/ DOI: 10.1242/jcs.110114
tissue_or_cell_type
Mitochondrial intermembrane space and cytosol
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 651–662
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Mammalian sulfite-oxidase targeting, cofactor depletion and maturation experiments · source_derived_draft · unverified_draft
### mo-suox-heme-order Heme binding occurred only after Moco integration in the studied SUOX maturation pathway. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Iron-containing heme is loaded after the molybdenum cofactor. organism: Mammalian/human cell models tissue_or_cell_type: Mitochondrial intermembrane space and cytosol experimental_model: Mammalian sulfite-oxidase targeting, cofactor depletion and maturation experiments limitations: Sequential maturation in the studied models; not a universal ranking of nutrient needs. exposure: Targeting-sequence constructs and absence of Moco evidence_span: {"source_cache": "artifacts/molybdenum-research/22854042.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "01970920183b87fde6830ca30d612aff75fc4b1a30672a3b9cc2f0c408294884", "start_char": 0, "end_char": 1268, "text_sha256": "01970920183b87fde6830ca30d612aff75fc4b1a30672a3b9cc2f0c408294884"} [mo-p22854042] Cofactor-dependent maturation of mammalian sulfite oxidase links two mitochondrial import pathways. (2012). https://pubmed.ncbi.nlm.nih.gov/22854042/ DOI: 10.1242/jcs.110114
Complete structured claim and evidence
SUOX dimerization did not occur in the absence of Moco and followed cofactor insertion.
Molybdenum cofactor / Moco → Sulfite oxidase homodimerization source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/22854042.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "01970920183b87fde6830ca30d612aff75fc4b1a30672a3b9cc2f0c408294884", "start_char": 0, "end_char": 1268, "text_sha256": "01970920183b87fde6830ca30d612aff75fc4b1a30672a3b9cc2f0c408294884"}
experimental_model
Mammalian sulfite-oxidase targeting, cofactor depletion and maturation experiments
exposure
Targeting-sequence constructs and absence of Moco
limitations
Sequential maturation in the studied models; not a universal ranking of nutrient needs.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Mammalian/human cell models
plain_language
The enzyme also needs cofactor loading before assembling its mature pair.
primary_references
[mo-p22854042] Cofactor-dependent maturation of mammalian sulfite oxidase links two mitochondrial import pathways. (2012). https://pubmed.ncbi.nlm.nih.gov/22854042/ DOI: 10.1242/jcs.110114
tissue_or_cell_type
Mitochondrial intermembrane space and cytosol
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 664–675
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Mammalian sulfite-oxidase targeting, cofactor depletion and maturation experiments · source_derived_draft · unverified_draft
### mo-suox-dimer-order SUOX dimerization did not occur in the absence of Moco and followed cofactor insertion. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The enzyme also needs cofactor loading before assembling its mature pair. organism: Mammalian/human cell models tissue_or_cell_type: Mitochondrial intermembrane space and cytosol experimental_model: Mammalian sulfite-oxidase targeting, cofactor depletion and maturation experiments limitations: Sequential maturation in the studied models; not a universal ranking of nutrient needs. exposure: Targeting-sequence constructs and absence of Moco evidence_span: {"source_cache": "artifacts/molybdenum-research/22854042.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "01970920183b87fde6830ca30d612aff75fc4b1a30672a3b9cc2f0c408294884", "start_char": 0, "end_char": 1268, "text_sha256": "01970920183b87fde6830ca30d612aff75fc4b1a30672a3b9cc2f0c408294884"} [mo-p22854042] Cofactor-dependent maturation of mammalian sulfite oxidase links two mitochondrial import pathways. (2012). https://pubmed.ncbi.nlm.nih.gov/22854042/ DOI: 10.1242/jcs.110114
Complete structured claim and evidence
Human CDO1 oxidizes cysteine to cysteine sulfinic acid using molecular oxygen and a non-heme iron center.
Human cysteine dioxygenase / CDO1 → L-Cysteine source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/17135237.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3ccd6f2de98887d17d935999238a88d8901fe8a66bb9b48c9cbd5d179bf180d6", "start_char": 0, "end_char": 1343, "text_sha256": "3ccd6f2de98887d17d935999238a88d8901fe8a66bb9b48c9cbd5d179bf180d6"}
experimental_model
Purified human CDO1 crystallography, substrate binding, metal analysis and mutants
exposure
L-cysteine oxidation with molecular oxygen
limitations
The overall reaction and iron requirement are recorded; disputed detailed structural intermediates are not assigned as settled.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
Iron-dependent CDO1 starts an upstream sulfur-breakdown route.
primary_references
[mo-p17135237] An insight into the mechanism of human cysteine dioxygenase. Key roles of the thioether-bonded tyrosine-cysteine cofactor. (2007). https://pubmed.ncbi.nlm.nih.gov/17135237/ DOI: 10.1074/jbc.m609337200
tissue_or_cell_type
Recombinant human cysteine dioxygenase
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 677–688
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human CDO1 crystallography, substrate binding, metal analysis and mutants · source_derived_draft · unverified_draft
### mo-cdo-csa Human CDO1 oxidizes cysteine to cysteine sulfinic acid using molecular oxygen and a non-heme iron center. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Iron-dependent CDO1 starts an upstream sulfur-breakdown route. organism: Homo sapiens tissue_or_cell_type: Recombinant human cysteine dioxygenase experimental_model: Purified human CDO1 crystallography, substrate binding, metal analysis and mutants limitations: The overall reaction and iron requirement are recorded; disputed detailed structural intermediates are not assigned as settled. exposure: L-cysteine oxidation with molecular oxygen evidence_span: {"source_cache": "artifacts/molybdenum-research/17135237.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3ccd6f2de98887d17d935999238a88d8901fe8a66bb9b48c9cbd5d179bf180d6", "start_char": 0, "end_char": 1343, "text_sha256": "3ccd6f2de98887d17d935999238a88d8901fe8a66bb9b48c9cbd5d179bf180d6"} [mo-p17135237] An insight into the mechanism of human cysteine dioxygenase. Key roles of the thioether-bonded tyrosine-cysteine cofactor. (2007). https://pubmed.ncbi.nlm.nih.gov/17135237/ DOI: 10.1074/jbc.m609337200
Complete structured claim and evidence
GOT1 was the principal contributor to cysteine-sulfinate conversion to sulfite and pyruvate in the studied human-cell system.
Human cytosolic aspartate aminotransferase / GOT1 → L-Cysteine sulfinic acid source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/33271457.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "619710a31160db0927e01193e458277773ebe5e5423629e7dab58888ab6bc617", "start_char": 0, "end_char": 1479, "text_sha256": "619710a31160db0927e01193e458277773ebe5e5423629e7dab58888ab6bc617"}
experimental_model
CRISPR SUOX/GOT1/GOT2 perturbations and sulfur-metabolite assays
exposure
Cysteine-sulfinate and H2S pathway experiments
limitations
Cell-specific contributions; a higher concentration is not a direct measurement of pathway flux.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
The B6-linked transaminase route can feed sulfur into SUOX.
primary_references
[mo-p33271457] The role of glutamate oxaloacetate transaminases in sulfite biosynthesis and H2S metabolism. (2021). https://pubmed.ncbi.nlm.nih.gov/33271457/ DOI: 10.1016/j.redox.2020.101800
tissue_or_cell_type
HEK293T cells
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 690–701
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · CRISPR SUOX/GOT1/GOT2 perturbations and sulfur-metabolite assays · source_derived_draft · unverified_draft
### mo-got1-sulfite GOT1 was the principal contributor to cysteine-sulfinate conversion to sulfite and pyruvate in the studied human-cell system. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The B6-linked transaminase route can feed sulfur into SUOX. organism: Homo sapiens tissue_or_cell_type: HEK293T cells experimental_model: CRISPR SUOX/GOT1/GOT2 perturbations and sulfur-metabolite assays limitations: Cell-specific contributions; a higher concentration is not a direct measurement of pathway flux. exposure: Cysteine-sulfinate and H2S pathway experiments evidence_span: {"source_cache": "artifacts/molybdenum-research/33271457.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "619710a31160db0927e01193e458277773ebe5e5423629e7dab58888ab6bc617", "start_char": 0, "end_char": 1479, "text_sha256": "619710a31160db0927e01193e458277773ebe5e5423629e7dab58888ab6bc617"} [mo-p33271457] The role of glutamate oxaloacetate transaminases in sulfite biosynthesis and H2S metabolism. (2021). https://pubmed.ncbi.nlm.nih.gov/33271457/ DOI: 10.1016/j.redox.2020.101800
Complete structured claim and evidence
SUOX deficiency was accompanied by increased H2S steady-state levels without upregulation of the known H2S-producing pathways.
Human sulfite oxidase / SUOX → Hydrogen sulfide / H2S source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/33271457.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "619710a31160db0927e01193e458277773ebe5e5423629e7dab58888ab6bc617", "start_char": 0, "end_char": 1479, "text_sha256": "619710a31160db0927e01193e458277773ebe5e5423629e7dab58888ab6bc617"}
experimental_model
CRISPR SUOX/GOT1/GOT2 perturbations and sulfur-metabolite assays
exposure
Cysteine-sulfinate and H2S pathway experiments
limitations
Cell-specific contributions; a higher concentration is not a direct measurement of pathway flux.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
The sulfur disturbance extends beyond sulfite, but its precise route remains unresolved.
primary_references
[mo-p33271457] The role of glutamate oxaloacetate transaminases in sulfite biosynthesis and H2S metabolism. (2021). https://pubmed.ncbi.nlm.nih.gov/33271457/ DOI: 10.1016/j.redox.2020.101800
tissue_or_cell_type
HEK293T cells
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 703–714
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · CRISPR SUOX/GOT1/GOT2 perturbations and sulfur-metabolite assays · source_derived_draft · unverified_draft
### mo-suox-h2s SUOX deficiency was accompanied by increased H2S steady-state levels without upregulation of the known H2S-producing pathways. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The sulfur disturbance extends beyond sulfite, but its precise route remains unresolved. organism: Homo sapiens tissue_or_cell_type: HEK293T cells experimental_model: CRISPR SUOX/GOT1/GOT2 perturbations and sulfur-metabolite assays limitations: Cell-specific contributions; a higher concentration is not a direct measurement of pathway flux. exposure: Cysteine-sulfinate and H2S pathway experiments evidence_span: {"source_cache": "artifacts/molybdenum-research/33271457.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "619710a31160db0927e01193e458277773ebe5e5423629e7dab58888ab6bc617", "start_char": 0, "end_char": 1479, "text_sha256": "619710a31160db0927e01193e458277773ebe5e5423629e7dab58888ab6bc617"} [mo-p33271457] The role of glutamate oxaloacetate transaminases in sulfite biosynthesis and H2S metabolism. (2021). https://pubmed.ncbi.nlm.nih.gov/33271457/ DOI: 10.1016/j.redox.2020.101800
Complete structured claim and evidence
SUOX-deficient cells accumulated persulfidated glutathione and cysteine.
Human sulfite oxidase / SUOX → Glutathione persulfide / GSSH source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/33271457.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "619710a31160db0927e01193e458277773ebe5e5423629e7dab58888ab6bc617", "start_char": 0, "end_char": 1479, "text_sha256": "619710a31160db0927e01193e458277773ebe5e5423629e7dab58888ab6bc617"}
experimental_model
CRISPR SUOX/GOT1/GOT2 perturbations and sulfur-metabolite assays
exposure
Cysteine-sulfinate and H2S pathway experiments
limitations
Cell-specific contributions; a higher concentration is not a direct measurement of pathway flux.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
Glutathione and cysteine sulfur chemistry also changed.
primary_references
[mo-p33271457] The role of glutamate oxaloacetate transaminases in sulfite biosynthesis and H2S metabolism. (2021). https://pubmed.ncbi.nlm.nih.gov/33271457/ DOI: 10.1016/j.redox.2020.101800
tissue_or_cell_type
HEK293T cells
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 716–727
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · CRISPR SUOX/GOT1/GOT2 perturbations and sulfur-metabolite assays · source_derived_draft · unverified_draft
### mo-suox-persulfides SUOX-deficient cells accumulated persulfidated glutathione and cysteine. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Glutathione and cysteine sulfur chemistry also changed. organism: Homo sapiens tissue_or_cell_type: HEK293T cells experimental_model: CRISPR SUOX/GOT1/GOT2 perturbations and sulfur-metabolite assays limitations: Cell-specific contributions; a higher concentration is not a direct measurement of pathway flux. exposure: Cysteine-sulfinate and H2S pathway experiments evidence_span: {"source_cache": "artifacts/molybdenum-research/33271457.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "619710a31160db0927e01193e458277773ebe5e5423629e7dab58888ab6bc617", "start_char": 0, "end_char": 1479, "text_sha256": "619710a31160db0927e01193e458277773ebe5e5423629e7dab58888ab6bc617"} [mo-p33271457] The role of glutamate oxaloacetate transaminases in sulfite biosynthesis and H2S metabolism. (2021). https://pubmed.ncbi.nlm.nih.gov/33271457/ DOI: 10.1016/j.redox.2020.101800
Complete structured claim and evidence
The sulfite-accumulating cells had increased SQOR protein levels.
Human sulfite oxidase / SUOX → Human sulfide:quinone oxidoreductase / SQOR source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/33271457.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "619710a31160db0927e01193e458277773ebe5e5423629e7dab58888ab6bc617", "start_char": 0, "end_char": 1479, "text_sha256": "619710a31160db0927e01193e458277773ebe5e5423629e7dab58888ab6bc617"}
experimental_model
CRISPR SUOX/GOT1/GOT2 perturbations and sulfur-metabolite assays
exposure
Cysteine-sulfinate and H2S pathway experiments
limitations
Cell-specific contributions; a higher concentration is not a direct measurement of pathway flux.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
A separate sulfur-oxidation enzyme responded to the disturbance.
primary_references
[mo-p33271457] The role of glutamate oxaloacetate transaminases in sulfite biosynthesis and H2S metabolism. (2021). https://pubmed.ncbi.nlm.nih.gov/33271457/ DOI: 10.1016/j.redox.2020.101800
tissue_or_cell_type
HEK293T cells
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 729–740
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · CRISPR SUOX/GOT1/GOT2 perturbations and sulfur-metabolite assays · source_derived_draft · unverified_draft
### mo-suox-sqor The sulfite-accumulating cells had increased SQOR protein levels. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: A separate sulfur-oxidation enzyme responded to the disturbance. organism: Homo sapiens tissue_or_cell_type: HEK293T cells experimental_model: CRISPR SUOX/GOT1/GOT2 perturbations and sulfur-metabolite assays limitations: Cell-specific contributions; a higher concentration is not a direct measurement of pathway flux. exposure: Cysteine-sulfinate and H2S pathway experiments evidence_span: {"source_cache": "artifacts/molybdenum-research/33271457.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "619710a31160db0927e01193e458277773ebe5e5423629e7dab58888ab6bc617", "start_char": 0, "end_char": 1479, "text_sha256": "619710a31160db0927e01193e458277773ebe5e5423629e7dab58888ab6bc617"} [mo-p33271457] The role of glutamate oxaloacetate transaminases in sulfite biosynthesis and H2S metabolism. (2021). https://pubmed.ncbi.nlm.nih.gov/33271457/ DOI: 10.1016/j.redox.2020.101800
Complete structured claim and evidence
The primary article describes sequential XOR hydroxylation of hypoxanthine to xanthine and xanthine to urate.
Human xanthine oxidoreductase / XDH → Hypoxanthine source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/37713777.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a8092b2aa7328b59f0275dd8a37d2a2dbb5abb2a32236d0cab5fffcc1ddc671d", "start_char": 1061, "end_char": 1244, "text_sha256": "45575621674b6b2e232b2e7b9605ad8e6acde4977d3f22e20abebfcbfa0b4dcb"}
experimental_model
Recombinant human XDH variants with urate, superoxide and NO assays
exposure
Xanthine, oxygen and inorganic nitrite assays
limitations
Established reaction summarized in the primary article background; this paper directly assayed xanthine-based activity rather than newly establishing the hypoxanthine step.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens protein
plain_language
Hypoxanthine enters the same two-step purine pathway.
primary_references
[mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? (2023). https://pubmed.ncbi.nlm.nih.gov/37713777/ DOI: 10.1016/j.redox.2023.102864
tissue_or_cell_type
Purified human enzyme
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 755–766
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human XDH variants with urate, superoxide and NO assays · source_derived_draft · unverified_draft
### mo-xdh-hypoxanthine The primary article describes sequential XOR hydroxylation of hypoxanthine to xanthine and xanthine to urate. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Hypoxanthine enters the same two-step purine pathway. organism: Homo sapiens protein tissue_or_cell_type: Purified human enzyme experimental_model: Recombinant human XDH variants with urate, superoxide and NO assays limitations: Established reaction summarized in the primary article background; this paper directly assayed xanthine-based activity rather than newly establishing the hypoxanthine step. exposure: Xanthine, oxygen and inorganic nitrite assays evidence_span: {"source_cache": "artifacts/molybdenum-research/37713777.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a8092b2aa7328b59f0275dd8a37d2a2dbb5abb2a32236d0cab5fffcc1ddc671d", "start_char": 1061, "end_char": 1244, "text_sha256": "45575621674b6b2e232b2e7b9605ad8e6acde4977d3f22e20abebfcbfa0b4dcb"} [mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? (2023). https://pubmed.ncbi.nlm.nih.gov/37713777/ DOI: 10.1016/j.redox.2023.102864
Complete structured claim and evidence
The XDH form transfers purine-derived electrons through its iron-sulfur centers and FAD to NAD+, producing NADH.
Human xanthine oxidoreductase / XDH → NAD+ source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/37713777.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a8092b2aa7328b59f0275dd8a37d2a2dbb5abb2a32236d0cab5fffcc1ddc671d", "start_char": 0, "end_char": 1579, "text_sha256": "18325172be489f8f4beae16c04dbc4f49f94c87186321e32aede61f27089c7c4"}
experimental_model
Recombinant human XDH variants with urate, superoxide and NO assays
exposure
Xanthine, oxygen and inorganic nitrite assays
limitations
Canonical electron-transfer mechanism stated in this primary article; not an experiment on dietary B2 or niacin depletion.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens protein
plain_language
Riboflavin-derived FAD, iron-sulfur centers and niacin-derived NAD work alongside molybdenum.
primary_references
[mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? (2023). https://pubmed.ncbi.nlm.nih.gov/37713777/ DOI: 10.1016/j.redox.2023.102864
tissue_or_cell_type
Purified human enzyme
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 768–779
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human XDH variants with urate, superoxide and NO assays · source_derived_draft · unverified_draft
### mo-xdh-nad The XDH form transfers purine-derived electrons through its iron-sulfur centers and FAD to NAD+, producing NADH. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Riboflavin-derived FAD, iron-sulfur centers and niacin-derived NAD work alongside molybdenum. organism: Homo sapiens protein tissue_or_cell_type: Purified human enzyme experimental_model: Recombinant human XDH variants with urate, superoxide and NO assays limitations: Canonical electron-transfer mechanism stated in this primary article; not an experiment on dietary B2 or niacin depletion. exposure: Xanthine, oxygen and inorganic nitrite assays evidence_span: {"source_cache": "artifacts/molybdenum-research/37713777.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a8092b2aa7328b59f0275dd8a37d2a2dbb5abb2a32236d0cab5fffcc1ddc671d", "start_char": 0, "end_char": 1579, "text_sha256": "18325172be489f8f4beae16c04dbc4f49f94c87186321e32aede61f27089c7c4"} [mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? (2023). https://pubmed.ncbi.nlm.nih.gov/37713777/ DOI: 10.1016/j.redox.2023.102864
Complete structured claim and evidence
In its oxidase activity, XOR can generate superoxide and hydrogen peroxide rather than exclusively transferring electrons to NAD+.
Human xanthine oxidoreductase / XDH → Superoxide radical anion source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/37713777.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9", "start_char": 0, "end_char": 1655, "text_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9"}
experimental_model
Recombinant human XDH variants with urate, superoxide and NO assays
exposure
Xanthine, oxygen and inorganic nitrite assays
limitations
The 2023 Fig. 6E corrigendum corrects a displayed panel; authors state data and conclusions are unchanged. Enzyme activity is not a clinical benefit or dietary response.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens protein
plain_language
The enzyme can generate oxidants as well as carry out purine breakdown.
primary_references
[mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? (2023). https://pubmed.ncbi.nlm.nih.gov/37713777/ DOI: 10.1016/j.redox.2023.102864
tissue_or_cell_type
Purified human enzyme
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 781–792
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human XDH variants with urate, superoxide and NO assays · source_derived_draft · unverified_draft
### mo-xor-oxygen In its oxidase activity, XOR can generate superoxide and hydrogen peroxide rather than exclusively transferring electrons to NAD+. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The enzyme can generate oxidants as well as carry out purine breakdown. organism: Homo sapiens protein tissue_or_cell_type: Purified human enzyme experimental_model: Recombinant human XDH variants with urate, superoxide and NO assays limitations: The 2023 Fig. 6E corrigendum corrects a displayed panel; authors state data and conclusions are unchanged. Enzyme activity is not a clinical benefit or dietary response. exposure: Xanthine, oxygen and inorganic nitrite assays evidence_span: {"source_cache": "artifacts/molybdenum-research/37713777.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9", "start_char": 0, "end_char": 1655, "text_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9"} [mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? (2023). https://pubmed.ncbi.nlm.nih.gov/37713777/ DOI: 10.1016/j.redox.2023.102864
Complete structured claim and evidence
Human XOR reduced nitrite to NO under the tested reducing conditions, and nitrite decreased XOR-driven superoxide production.
Human xanthine oxidoreductase / XDH → Nitrite / NO2(-) source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/37713777.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9", "start_char": 0, "end_char": 1655, "text_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9"}
experimental_model
Recombinant human XDH variants with urate, superoxide and NO assays
exposure
Xanthine, oxygen and inorganic nitrite assays
limitations
The 2023 Fig. 6E corrigendum corrects a displayed panel; authors state data and conclusions are unchanged. Enzyme activity is not a clinical benefit or dietary response.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens protein
plain_language
Changing the available electron acceptor changed the products.
primary_references
[mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? (2023). https://pubmed.ncbi.nlm.nih.gov/37713777/ DOI: 10.1016/j.redox.2023.102864
tissue_or_cell_type
Purified human enzyme
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 794–805
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human XDH variants with urate, superoxide and NO assays · source_derived_draft · unverified_draft
### mo-xor-nitrite Human XOR reduced nitrite to NO under the tested reducing conditions, and nitrite decreased XOR-driven superoxide production. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Changing the available electron acceptor changed the products. organism: Homo sapiens protein tissue_or_cell_type: Purified human enzyme experimental_model: Recombinant human XDH variants with urate, superoxide and NO assays limitations: The 2023 Fig. 6E corrigendum corrects a displayed panel; authors state data and conclusions are unchanged. Enzyme activity is not a clinical benefit or dietary response. exposure: Xanthine, oxygen and inorganic nitrite assays evidence_span: {"source_cache": "artifacts/molybdenum-research/37713777.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9", "start_char": 0, "end_char": 1655, "text_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9"} [mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? (2023). https://pubmed.ncbi.nlm.nih.gov/37713777/ DOI: 10.1016/j.redox.2023.102864
Complete structured claim and evidence
His1221Arg increased urate, superoxide and NO formation relative to wild type in xanthine-supplied assays.
Human XDH p.His1221Arg → Urate / uric acid source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/37713777.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9", "start_char": 0, "end_char": 1655, "text_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9"}
experimental_model
Recombinant human XDH variants with urate, superoxide and NO assays
exposure
Xanthine, oxygen and inorganic nitrite assays
limitations
The 2023 Fig. 6E corrigendum corrects a displayed panel; authors state data and conclusions are unchanged. Enzyme activity is not a clinical benefit or dietary response.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens protein
plain_language
One variant raised several outputs at once.
primary_references
[mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? (2023). https://pubmed.ncbi.nlm.nih.gov/37713777/ DOI: 10.1016/j.redox.2023.102864
tissue_or_cell_type
Purified human enzyme
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 807–818
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human XDH variants with urate, superoxide and NO assays · source_derived_draft · unverified_draft
### mo-xor-h1221r His1221Arg increased urate, superoxide and NO formation relative to wild type in xanthine-supplied assays. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: One variant raised several outputs at once. organism: Homo sapiens protein tissue_or_cell_type: Purified human enzyme experimental_model: Recombinant human XDH variants with urate, superoxide and NO assays limitations: The 2023 Fig. 6E corrigendum corrects a displayed panel; authors state data and conclusions are unchanged. Enzyme activity is not a clinical benefit or dietary response. exposure: Xanthine, oxygen and inorganic nitrite assays evidence_span: {"source_cache": "artifacts/molybdenum-research/37713777.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9", "start_char": 0, "end_char": 1655, "text_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9"} [mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? (2023). https://pubmed.ncbi.nlm.nih.gov/37713777/ DOI: 10.1016/j.redox.2023.102864
Complete structured claim and evidence
Ile703Val increased urate and NO formation without increasing superoxide formation in the reported comparison.
Human XDH p.Ile703Val → Urate / uric acid source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/37713777.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9", "start_char": 0, "end_char": 1655, "text_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9"}
experimental_model
Recombinant human XDH variants with urate, superoxide and NO assays
exposure
Xanthine, oxygen and inorganic nitrite assays
limitations
The 2023 Fig. 6E corrigendum corrects a displayed panel; authors state data and conclusions are unchanged. Enzyme activity is not a clinical benefit or dietary response.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens protein
plain_language
Another variant changed the balance of products differently.
primary_references
[mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? (2023). https://pubmed.ncbi.nlm.nih.gov/37713777/ DOI: 10.1016/j.redox.2023.102864
tissue_or_cell_type
Purified human enzyme
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 820–831
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human XDH variants with urate, superoxide and NO assays · source_derived_draft · unverified_draft
### mo-xor-i703v Ile703Val increased urate and NO formation without increasing superoxide formation in the reported comparison. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Another variant changed the balance of products differently. organism: Homo sapiens protein tissue_or_cell_type: Purified human enzyme experimental_model: Recombinant human XDH variants with urate, superoxide and NO assays limitations: The 2023 Fig. 6E corrigendum corrects a displayed panel; authors state data and conclusions are unchanged. Enzyme activity is not a clinical benefit or dietary response. exposure: Xanthine, oxygen and inorganic nitrite assays evidence_span: {"source_cache": "artifacts/molybdenum-research/37713777.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9", "start_char": 0, "end_char": 1655, "text_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9"} [mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? (2023). https://pubmed.ncbi.nlm.nih.gov/37713777/ DOI: 10.1016/j.redox.2023.102864
Complete structured claim and evidence
Thioridazine bound a distinct noncompetitive inhibitor site in human AOX1.
Thioridazine → Human aldehyde oxidase 1 / AOX1 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/26322824.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0c289f1d166c7335431b4d041963accf22af348b4cac506145f2ccef59ca8188", "start_char": 0, "end_char": 1067, "text_sha256": "0c289f1d166c7335431b4d041963accf22af348b4cac506145f2ccef59ca8188"}
experimental_model
Human AOX1 structures and steady-state kinetics with substrate and inhibitor
exposure
Phthalazine and thioridazine
limitations
Specific xenobiotic chemistry; does not establish broad detoxification benefits from molybdenum supplements.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens protein
plain_language
A drug can inhibit AOX1 at a site separate from its substrate reaction.
primary_references
[mo-p26322824] Structural insights into xenobiotic and inhibitor binding to human aldehyde oxidase. (2015). https://pubmed.ncbi.nlm.nih.gov/26322824/ DOI: 10.1038/nchembio.1895
tissue_or_cell_type
Recombinant purified AOX1
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 846–857
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human AOX1 structures and steady-state kinetics with substrate and inhibitor · source_derived_draft · unverified_draft
### mo-aox-inhibition Thioridazine bound a distinct noncompetitive inhibitor site in human AOX1. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: A drug can inhibit AOX1 at a site separate from its substrate reaction. organism: Homo sapiens protein tissue_or_cell_type: Recombinant purified AOX1 experimental_model: Human AOX1 structures and steady-state kinetics with substrate and inhibitor limitations: Specific xenobiotic chemistry; does not establish broad detoxification benefits from molybdenum supplements. exposure: Phthalazine and thioridazine evidence_span: {"source_cache": "artifacts/molybdenum-research/26322824.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0c289f1d166c7335431b4d041963accf22af348b4cac506145f2ccef59ca8188", "start_char": 0, "end_char": 1067, "text_sha256": "0c289f1d166c7335431b4d041963accf22af348b4cac506145f2ccef59ca8188"} [mo-p26322824] Structural insights into xenobiotic and inhibitor binding to human aldehyde oxidase. (2015). https://pubmed.ncbi.nlm.nih.gov/26322824/ DOI: 10.1038/nchembio.1895
Complete structured claim and evidence
AOX1-bound FAD acted as the intrinsic fluorescence reporter in ThermoFAD unfolding assays.
FAD → Human aldehyde oxidase 1 / AOX1 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/30985987.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d187787b0c042c674903c56275b485ee23c2b3545ed1c0ed02ca0cd2e3abb7c0", "start_char": 11532, "end_char": 12101, "text_sha256": "13ae767e495f8efc3a6c44005156563bc471d8aec37486330086d3fed343ef38"}
experimental_model
Human AOX1 variant crystallography and CD/ThermoFAD stability assays
exposure
Wild type compared with SNP variants
limitations
In-vitro structures and thermal stability; not physiological temperature or diet thresholds.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens protein
plain_language
The molybdenum enzyme also contains a riboflavin-derived cofactor.
primary_references
[mo-p30985987] Human aldehyde oxidase (hAOX1): structure determination of the Moco-free form of the natural variant G1269R and biophysical studies of single nucleotide polymorphisms. (2019). https://pubmed.ncbi.nlm.nih.gov/30985987/ DOI: 10.1002/2211-5463.12617
tissue_or_cell_type
Purified AOX1
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 859–870
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human AOX1 variant crystallography and CD/ThermoFAD stability assays · source_derived_draft · unverified_draft
### mo-aox-fad AOX1-bound FAD acted as the intrinsic fluorescence reporter in ThermoFAD unfolding assays. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The molybdenum enzyme also contains a riboflavin-derived cofactor. organism: Homo sapiens protein tissue_or_cell_type: Purified AOX1 experimental_model: Human AOX1 variant crystallography and CD/ThermoFAD stability assays limitations: In-vitro structures and thermal stability; not physiological temperature or diet thresholds. exposure: Wild type compared with SNP variants evidence_span: {"source_cache": "artifacts/molybdenum-research/30985987.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d187787b0c042c674903c56275b485ee23c2b3545ed1c0ed02ca0cd2e3abb7c0", "start_char": 11532, "end_char": 12101, "text_sha256": "13ae767e495f8efc3a6c44005156563bc471d8aec37486330086d3fed343ef38"} [mo-p30985987] Human aldehyde oxidase (hAOX1): structure determination of the Moco-free form of the natural variant G1269R and biophysical studies of single nucleotide polymorphisms. (2019). https://pubmed.ncbi.nlm.nih.gov/30985987/ DOI: 10.1002/2211-5463.12617
Complete structured claim and evidence
The inactive AOX1 G1269R crystal structure lacked the entire Moco cofactor.
Human AOX1 p.Gly1269Arg → Molybdenum cofactor / Moco source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/30985987.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5442ecc25ebcf48ef56cc840357bfe9f233c2c9738d5e6b685db86aed2249fe0", "start_char": 0, "end_char": 1497, "text_sha256": "5442ecc25ebcf48ef56cc840357bfe9f233c2c9738d5e6b685db86aed2249fe0"}
experimental_model
Human AOX1 variant crystallography and CD/ThermoFAD stability assays
exposure
Wild type compared with SNP variants
limitations
In-vitro structures and thermal stability; not physiological temperature or diet thresholds.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens protein
plain_language
Protein presence alone did not guarantee a working enzyme.
primary_references
[mo-p30985987] Human aldehyde oxidase (hAOX1): structure determination of the Moco-free form of the natural variant G1269R and biophysical studies of single nucleotide polymorphisms. (2019). https://pubmed.ncbi.nlm.nih.gov/30985987/ DOI: 10.1002/2211-5463.12617
tissue_or_cell_type
Purified AOX1
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 872–883
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human AOX1 variant crystallography and CD/ThermoFAD stability assays · source_derived_draft · unverified_draft
### mo-aox-g1269r The inactive AOX1 G1269R crystal structure lacked the entire Moco cofactor. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Protein presence alone did not guarantee a working enzyme. organism: Homo sapiens protein tissue_or_cell_type: Purified AOX1 experimental_model: Human AOX1 variant crystallography and CD/ThermoFAD stability assays limitations: In-vitro structures and thermal stability; not physiological temperature or diet thresholds. exposure: Wild type compared with SNP variants evidence_span: {"source_cache": "artifacts/molybdenum-research/30985987.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5442ecc25ebcf48ef56cc840357bfe9f233c2c9738d5e6b685db86aed2249fe0", "start_char": 0, "end_char": 1497, "text_sha256": "5442ecc25ebcf48ef56cc840357bfe9f233c2c9738d5e6b685db86aed2249fe0"} [mo-p30985987] Human aldehyde oxidase (hAOX1): structure determination of the Moco-free form of the natural variant G1269R and biophysical studies of single nucleotide polymorphisms. (2019). https://pubmed.ncbi.nlm.nih.gov/30985987/ DOI: 10.1002/2211-5463.12617
Complete structured claim and evidence
A separable aldehyde-oxidase fraction accounted for some NAD-independent retinaldehyde metabolism in human liver and kidney extracts.
Human aldehyde oxidase 1 / AOX1 → Hepatic retinal oxidase activity source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/10559215.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a0a70e022e9499ca5d0608c1da80afadfad2215ac6cf1219c8ce8da3280a5238", "start_char": 0, "end_char": 1879, "text_sha256": "a0a70e022e9499ca5d0608c1da80afadfad2215ac6cf1219c8ce8da3280a5238"}
experimental_model
Biochemical fractionation of four human livers and three kidneys
exposure
Retinaldehyde and other aldehyde substrate assays
limitations
Biochemical enzyme-fraction identification predates modern isoform assays; does not establish AOX1 as the dominant human retinoic-acid source or mineral-responsive route.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
AOX1 intersects vitamin A chemistry, alongside other enzymes.
primary_references
[mo-p10559215] Metabolism of retinaldehyde and other aldehydes in soluble extracts of human liver and kidney. (1999). https://pubmed.ncbi.nlm.nih.gov/10559215/ DOI: 10.1074/jbc.274.47.33366
tissue_or_cell_type
Liver and kidney soluble extracts
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 885–896
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Biochemical fractionation of four human livers and three kidneys · source_derived_draft · unverified_draft
### mo-aox-retinal A separable aldehyde-oxidase fraction accounted for some NAD-independent retinaldehyde metabolism in human liver and kidney extracts. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: AOX1 intersects vitamin A chemistry, alongside other enzymes. organism: Homo sapiens tissue_or_cell_type: Liver and kidney soluble extracts experimental_model: Biochemical fractionation of four human livers and three kidneys limitations: Biochemical enzyme-fraction identification predates modern isoform assays; does not establish AOX1 as the dominant human retinoic-acid source or mineral-responsive route. exposure: Retinaldehyde and other aldehyde substrate assays evidence_span: {"source_cache": "artifacts/molybdenum-research/10559215.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a0a70e022e9499ca5d0608c1da80afadfad2215ac6cf1219c8ce8da3280a5238", "start_char": 0, "end_char": 1879, "text_sha256": "a0a70e022e9499ca5d0608c1da80afadfad2215ac6cf1219c8ce8da3280a5238"} [mo-p10559215] Metabolism of retinaldehyde and other aldehydes in soluble extracts of human liver and kidney. (1999). https://pubmed.ncbi.nlm.nih.gov/10559215/ DOI: 10.1074/jbc.274.47.33366
Complete structured claim and evidence
Recombinant human AOX converted all-trans-retinaldehyde to all-trans-retinoic acid, with an apparent Km near 1.5 micromolar.
Human aldehyde oxidase 1 / AOX1 → All-trans-retinal source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/33355213.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0edb31bff85231dfbde4a99d6858db611c099d2cd00982cad88616aa960b5aa2", "start_char": 0, "end_char": 2211, "text_sha256": "0edb31bff85231dfbde4a99d6858db611c099d2cd00982cad88616aa960b5aa2"}
experimental_model
Recombinant human AOX and human liver S9 kinetics, inhibitors and protein quantification
exposure
Retinaldehyde with/without NAD+; selective inhibitors
limitations
Ex-vivo contribution depends on substrate and NAD+ availability; no dietary molybdenum intervention or universal in-vivo percentage.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
A molybdenum enzyme can contribute to making vitamin A signaling molecules.
primary_references
[mo-p33355213] Aldehyde Oxidase Contributes to All-Trans-Retinoic Acid Biosynthesis in Human Liver. (2021). https://pubmed.ncbi.nlm.nih.gov/33355213/ DOI: 10.1124/dmd.120.000296
tissue_or_cell_type
Purified enzyme and liver S9 fractions
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 898–909
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human AOX and human liver S9 kinetics, inhibitors and protein quantification · source_derived_draft · unverified_draft
### mo-aox-retinoic-acid Recombinant human AOX converted all-trans-retinaldehyde to all-trans-retinoic acid, with an apparent Km near 1.5 micromolar. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: A molybdenum enzyme can contribute to making vitamin A signaling molecules. organism: Homo sapiens tissue_or_cell_type: Purified enzyme and liver S9 fractions experimental_model: Recombinant human AOX and human liver S9 kinetics, inhibitors and protein quantification limitations: Ex-vivo contribution depends on substrate and NAD+ availability; no dietary molybdenum intervention or universal in-vivo percentage. exposure: Retinaldehyde with/without NAD+; selective inhibitors evidence_span: {"source_cache": "artifacts/molybdenum-research/33355213.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0edb31bff85231dfbde4a99d6858db611c099d2cd00982cad88616aa960b5aa2", "start_char": 0, "end_char": 2211, "text_sha256": "0edb31bff85231dfbde4a99d6858db611c099d2cd00982cad88616aa960b5aa2"} [mo-p33355213] Aldehyde Oxidase Contributes to All-Trans-Retinoic Acid Biosynthesis in Human Liver. (2021). https://pubmed.ncbi.nlm.nih.gov/33355213/ DOI: 10.1124/dmd.120.000296
Complete structured claim and evidence
In human liver S9, AOX inhibition reduced retinoic-acid formation by 20-50%, versus 50-80% with ALDH1A1 inhibition; AOX had lower affinity and higher capacity.
Human aldehyde oxidase 1 / AOX1 → Aldehyde dehydrogenase 1A1 / ALDH1A1 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/33355213.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0edb31bff85231dfbde4a99d6858db611c099d2cd00982cad88616aa960b5aa2", "start_char": 0, "end_char": 2211, "text_sha256": "0edb31bff85231dfbde4a99d6858db611c099d2cd00982cad88616aa960b5aa2"}
experimental_model
Recombinant human AOX and human liver S9 kinetics, inhibitors and protein quantification
exposure
Retinaldehyde with/without NAD+; selective inhibitors
limitations
Ex-vivo contribution depends on substrate and NAD+ availability; no dietary molybdenum intervention or universal in-vivo percentage.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
Different enzymes share vitamin A processing, and their contributions depend on the conditions.
primary_references
[mo-p33355213] Aldehyde Oxidase Contributes to All-Trans-Retinoic Acid Biosynthesis in Human Liver. (2021). https://pubmed.ncbi.nlm.nih.gov/33355213/ DOI: 10.1124/dmd.120.000296
tissue_or_cell_type
Purified enzyme and liver S9 fractions
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 911–922
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human AOX and human liver S9 kinetics, inhibitors and protein quantification · source_derived_draft · unverified_draft
### mo-aox-aldh-partition In human liver S9, AOX inhibition reduced retinoic-acid formation by 20-50%, versus 50-80% with ALDH1A1 inhibition; AOX had lower affinity and higher capacity. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Different enzymes share vitamin A processing, and their contributions depend on the conditions. organism: Homo sapiens tissue_or_cell_type: Purified enzyme and liver S9 fractions experimental_model: Recombinant human AOX and human liver S9 kinetics, inhibitors and protein quantification limitations: Ex-vivo contribution depends on substrate and NAD+ availability; no dietary molybdenum intervention or universal in-vivo percentage. exposure: Retinaldehyde with/without NAD+; selective inhibitors evidence_span: {"source_cache": "artifacts/molybdenum-research/33355213.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0edb31bff85231dfbde4a99d6858db611c099d2cd00982cad88616aa960b5aa2", "start_char": 0, "end_char": 2211, "text_sha256": "0edb31bff85231dfbde4a99d6858db611c099d2cd00982cad88616aa960b5aa2"} [mo-p33355213] Aldehyde Oxidase Contributes to All-Trans-Retinoic Acid Biosynthesis in Human Liver. (2021). https://pubmed.ncbi.nlm.nih.gov/33355213/ DOI: 10.1124/dmd.120.000296
Complete structured claim and evidence
Inhibitor and fractionation experiments implicated AO and carboxylesterase, but not XOR, in GDC-0834 amide hydrolysis.
Human aldehyde oxidase 1 / AOX1 → GDC-0834 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/25845827.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8f5a9632067829ecae57508a9127fb042a6467165c3fc494fdd44be975dadf40", "start_char": 0, "end_char": 1619, "text_sha256": "8f5a9632067829ecae57508a9127fb042a6467165c3fc494fdd44be975dadf40"}
experimental_model
Human liver cytosolic fractionation, proteomics, inhibitors and docking
exposure
GDC-0834 amide-hydrolysis assays
limitations
AO and carboxylesterase both implicated; docking proposes a mechanism but does not prove every catalytic step.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
AOX1 can participate in drug breakdown beyond simple aldehyde oxidation.
primary_references
[mo-p25845827] A novel reaction mediated by human aldehyde oxidase: amide hydrolysis of GDC-0834. (2015). https://pubmed.ncbi.nlm.nih.gov/25845827/ DOI: 10.1124/dmd.114.061804
tissue_or_cell_type
Liver cytosol
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 924–935
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human liver cytosolic fractionation, proteomics, inhibitors and docking · source_derived_draft · unverified_draft
### mo-aox-amide Inhibitor and fractionation experiments implicated AO and carboxylesterase, but not XOR, in GDC-0834 amide hydrolysis. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: AOX1 can participate in drug breakdown beyond simple aldehyde oxidation. organism: Homo sapiens tissue_or_cell_type: Liver cytosol experimental_model: Human liver cytosolic fractionation, proteomics, inhibitors and docking limitations: AO and carboxylesterase both implicated; docking proposes a mechanism but does not prove every catalytic step. exposure: GDC-0834 amide-hydrolysis assays evidence_span: {"source_cache": "artifacts/molybdenum-research/25845827.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8f5a9632067829ecae57508a9127fb042a6467165c3fc494fdd44be975dadf40", "start_char": 0, "end_char": 1619, "text_sha256": "8f5a9632067829ecae57508a9127fb042a6467165c3fc494fdd44be975dadf40"} [mo-p25845827] A novel reaction mediated by human aldehyde oxidase: amide hydrolysis of GDC-0834. (2015). https://pubmed.ncbi.nlm.nih.gov/25845827/ DOI: 10.1124/dmd.114.061804
Complete structured claim and evidence
The reconstituted mARC system used NADH/FAD-dependent cytochrome b5 reductase and heme-containing cytochrome b5.
Human NADH-cytochrome b5 reductase / CYB5R3 → Human mitochondrial amidoxime-reducing component 1 / MTARC1 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/20861021.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0f430936dcc4701e5d57040edcab4b0418e3c49c59620e0f7d5f54aff41e7877", "start_char": 0, "end_char": 1557, "text_sha256": "0f430936dcc4701e5d57040edcab4b0418e3c49c59620e0f7d5f54aff41e7877"}
experimental_model
Recombinant human mARC1/mARC2 biochemical and spectroscopic reconstitution
exposure
N-hydroxylated substrates; cofactor reconstitution
limitations
The 2010 paper could not identify the Mo-ligating cysteine; later structural/mutagenesis work resolves that point. Its earlier inference is not imported as current fact.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Human proteins expressed in Escherichia coli
plain_language
Niacin, riboflavin, iron and molybdenum meet in one electron-transfer chain.
primary_references
[mo-p20861021] Biochemical and spectroscopic characterization of the human mitochondrial amidoxime reducing components hmARC-1 and hmARC-2 suggests the existence of a new molybdenum enzyme family in eukaryotes. (2010). https://pubmed.ncbi.nlm.nih.gov/20861021/ DOI: 10.1074/jbc.m110.169532
tissue_or_cell_type
Purified enzyme system
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 963–974
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human mARC1/mARC2 biochemical and spectroscopic reconstitution · source_derived_draft · unverified_draft
### mo-marc-fad-nadh The reconstituted mARC system used NADH/FAD-dependent cytochrome b5 reductase and heme-containing cytochrome b5. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Niacin, riboflavin, iron and molybdenum meet in one electron-transfer chain. organism: Human proteins expressed in Escherichia coli tissue_or_cell_type: Purified enzyme system experimental_model: Recombinant human mARC1/mARC2 biochemical and spectroscopic reconstitution limitations: The 2010 paper could not identify the Mo-ligating cysteine; later structural/mutagenesis work resolves that point. Its earlier inference is not imported as current fact. exposure: N-hydroxylated substrates; cofactor reconstitution evidence_span: {"source_cache": "artifacts/molybdenum-research/20861021.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0f430936dcc4701e5d57040edcab4b0418e3c49c59620e0f7d5f54aff41e7877", "start_char": 0, "end_char": 1557, "text_sha256": "0f430936dcc4701e5d57040edcab4b0418e3c49c59620e0f7d5f54aff41e7877"} [mo-p20861021] Biochemical and spectroscopic characterization of the human mitochondrial amidoxime reducing components hmARC-1 and hmARC-2 suggests the existence of a new molybdenum enzyme family in eukaryotes. (2010). https://pubmed.ncbi.nlm.nih.gov/20861021/ DOI: 10.1074/jbc.m110.169532
Complete structured claim and evidence
Active mARC1 and mARC2 were reconstituted with Moco without the terminal sulfuration needed by the XOR enzyme family.
Molybdenum cofactor / Moco → Human mitochondrial amidoxime-reducing component 1 / MTARC1 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/20861021.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0f430936dcc4701e5d57040edcab4b0418e3c49c59620e0f7d5f54aff41e7877", "start_char": 0, "end_char": 1557, "text_sha256": "0f430936dcc4701e5d57040edcab4b0418e3c49c59620e0f7d5f54aff41e7877"}
experimental_model
Recombinant human mARC1/mARC2 biochemical and spectroscopic reconstitution
exposure
N-hydroxylated substrates; cofactor reconstitution
limitations
The 2010 paper could not identify the Mo-ligating cysteine; later structural/mutagenesis work resolves that point. Its earlier inference is not imported as current fact.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Human proteins expressed in Escherichia coli
plain_language
mARC does not require the extra sulfur-activation step used by XDH and AOX1.
primary_references
[mo-p20861021] Biochemical and spectroscopic characterization of the human mitochondrial amidoxime reducing components hmARC-1 and hmARC-2 suggests the existence of a new molybdenum enzyme family in eukaryotes. (2010). https://pubmed.ncbi.nlm.nih.gov/20861021/ DOI: 10.1074/jbc.m110.169532
tissue_or_cell_type
Purified enzyme system
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 976–987
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human mARC1/mARC2 biochemical and spectroscopic reconstitution · source_derived_draft · unverified_draft
### mo-marc-no-terminal-sulfur Active mARC1 and mARC2 were reconstituted with Moco without the terminal sulfuration needed by the XOR enzyme family. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: mARC does not require the extra sulfur-activation step used by XDH and AOX1. organism: Human proteins expressed in Escherichia coli tissue_or_cell_type: Purified enzyme system experimental_model: Recombinant human mARC1/mARC2 biochemical and spectroscopic reconstitution limitations: The 2010 paper could not identify the Mo-ligating cysteine; later structural/mutagenesis work resolves that point. Its earlier inference is not imported as current fact. exposure: N-hydroxylated substrates; cofactor reconstitution evidence_span: {"source_cache": "artifacts/molybdenum-research/20861021.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0f430936dcc4701e5d57040edcab4b0418e3c49c59620e0f7d5f54aff41e7877", "start_char": 0, "end_char": 1557, "text_sha256": "0f430936dcc4701e5d57040edcab4b0418e3c49c59620e0f7d5f54aff41e7877"} [mo-p20861021] Biochemical and spectroscopic characterization of the human mitochondrial amidoxime reducing components hmARC-1 and hmARC-2 suggests the existence of a new molybdenum enzyme family in eukaryotes. (2010). https://pubmed.ncbi.nlm.nih.gov/20861021/ DOI: 10.1074/jbc.m110.169532
Complete structured claim and evidence
Mitochondrial CYB5B was required for the mARC-containing N-reductive system in the studied human cells.
Human mitochondrial cytochrome b5 / CYB5B → Human mitochondrial amidoxime-reducing component 1 / MTARC1 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/23703616.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9034da6c790ca6e0c60dd765eec631ea2875c6caf65f6d15d59733bc5e0ee0ec", "start_char": 0, "end_char": 1596, "text_sha256": "9034da6c790ca6e0c60dd765eec631ea2875c6caf65f6d15d59733bc5e0ee0ec"}
experimental_model
Human-cell siRNA plus recombinant cytochrome-b5/cofactor reconstitution
exposure
mARC, CYB5B and CYB5A depletion; apo-CYB5
limitations
Expression-dependent cellular contributions; no clinical iron or B2 supplementation test.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens; separate mouse Cyb5a knockout
plain_language
mARC needs an electron-delivery partner.
primary_references
[mo-p23703616] The involvement of mitochondrial amidoxime reducing components 1 and 2 and mitochondrial cytochrome b5 in N-reductive metabolism in human cells. (2013). https://pubmed.ncbi.nlm.nih.gov/23703616/ DOI: 10.1074/jbc.m113.474916
tissue_or_cell_type
HEK293 and second human cell line; purified proteins
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 989–1000
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human-cell siRNA plus recombinant cytochrome-b5/cofactor reconstitution · source_derived_draft · unverified_draft
### mo-cyb5b-marc Mitochondrial CYB5B was required for the mARC-containing N-reductive system in the studied human cells. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: mARC needs an electron-delivery partner. organism: Homo sapiens; separate mouse Cyb5a knockout tissue_or_cell_type: HEK293 and second human cell line; purified proteins experimental_model: Human-cell siRNA plus recombinant cytochrome-b5/cofactor reconstitution limitations: Expression-dependent cellular contributions; no clinical iron or B2 supplementation test. exposure: mARC, CYB5B and CYB5A depletion; apo-CYB5 evidence_span: {"source_cache": "artifacts/molybdenum-research/23703616.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9034da6c790ca6e0c60dd765eec631ea2875c6caf65f6d15d59733bc5e0ee0ec", "start_char": 0, "end_char": 1596, "text_sha256": "9034da6c790ca6e0c60dd765eec631ea2875c6caf65f6d15d59733bc5e0ee0ec"} [mo-p23703616] The involvement of mitochondrial amidoxime reducing components 1 and 2 and mitochondrial cytochrome b5 in N-reductive metabolism in human cells. (2013). https://pubmed.ncbi.nlm.nih.gov/23703616/ DOI: 10.1074/jbc.m113.474916
Complete structured claim and evidence
Heme-free apo-CYB5 failed to support N-reduction in the reconstituted system.
Heme → Human mitochondrial cytochrome b5 / CYB5B source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/23703616.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9034da6c790ca6e0c60dd765eec631ea2875c6caf65f6d15d59733bc5e0ee0ec", "start_char": 0, "end_char": 1596, "text_sha256": "9034da6c790ca6e0c60dd765eec631ea2875c6caf65f6d15d59733bc5e0ee0ec"}
experimental_model
Human-cell siRNA plus recombinant cytochrome-b5/cofactor reconstitution
exposure
mARC, CYB5B and CYB5A depletion; apo-CYB5
limitations
Expression-dependent cellular contributions; no clinical iron or B2 supplementation test.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens; separate mouse Cyb5a knockout
plain_language
Removing the iron-containing heme breaks this electron-transfer step.
primary_references
[mo-p23703616] The involvement of mitochondrial amidoxime reducing components 1 and 2 and mitochondrial cytochrome b5 in N-reductive metabolism in human cells. (2013). https://pubmed.ncbi.nlm.nih.gov/23703616/ DOI: 10.1074/jbc.m113.474916
tissue_or_cell_type
HEK293 and second human cell line; purified proteins
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1002–1013
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human-cell siRNA plus recombinant cytochrome-b5/cofactor reconstitution · source_derived_draft · unverified_draft
### mo-cyb5b-heme Heme-free apo-CYB5 failed to support N-reduction in the reconstituted system. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Removing the iron-containing heme breaks this electron-transfer step. organism: Homo sapiens; separate mouse Cyb5a knockout tissue_or_cell_type: HEK293 and second human cell line; purified proteins experimental_model: Human-cell siRNA plus recombinant cytochrome-b5/cofactor reconstitution limitations: Expression-dependent cellular contributions; no clinical iron or B2 supplementation test. exposure: mARC, CYB5B and CYB5A depletion; apo-CYB5 evidence_span: {"source_cache": "artifacts/molybdenum-research/23703616.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9034da6c790ca6e0c60dd765eec631ea2875c6caf65f6d15d59733bc5e0ee0ec", "start_char": 0, "end_char": 1596, "text_sha256": "9034da6c790ca6e0c60dd765eec631ea2875c6caf65f6d15d59733bc5e0ee0ec"} [mo-p23703616] The involvement of mitochondrial amidoxime reducing components 1 and 2 and mitochondrial cytochrome b5 in N-reductive metabolism in human cells. (2013). https://pubmed.ncbi.nlm.nih.gov/23703616/ DOI: 10.1074/jbc.m113.474916
Complete structured claim and evidence
CYB5A siRNA in HEK293 cells and Cyb5a knockout in mice did not support a required role for the microsomal isoform in measured N-reduction.
Human microsomal cytochrome b5 / CYB5A → Human mitochondrial amidoxime-reducing component 1 / MTARC1 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/23703616.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9034da6c790ca6e0c60dd765eec631ea2875c6caf65f6d15d59733bc5e0ee0ec", "start_char": 0, "end_char": 1596, "text_sha256": "9034da6c790ca6e0c60dd765eec631ea2875c6caf65f6d15d59733bc5e0ee0ec"}
experimental_model
Human-cell siRNA plus recombinant cytochrome-b5/cofactor reconstitution
exposure
mARC, CYB5B and CYB5A depletion; apo-CYB5
limitations
Expression-dependent cellular contributions; no clinical iron or B2 supplementation test.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens; separate mouse Cyb5a knockout
plain_language
The location and identity of the cytochrome b5 partner matter.
primary_references
[mo-p23703616] The involvement of mitochondrial amidoxime reducing components 1 and 2 and mitochondrial cytochrome b5 in N-reductive metabolism in human cells. (2013). https://pubmed.ncbi.nlm.nih.gov/23703616/ DOI: 10.1074/jbc.m113.474916
tissue_or_cell_type
HEK293 and second human cell line; purified proteins
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1015–1026
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human-cell siRNA plus recombinant cytochrome-b5/cofactor reconstitution · source_derived_draft · unverified_draft
### mo-cyb5a-not-substitute CYB5A siRNA in HEK293 cells and Cyb5a knockout in mice did not support a required role for the microsomal isoform in measured N-reduction. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The location and identity of the cytochrome b5 partner matter. organism: Homo sapiens; separate mouse Cyb5a knockout tissue_or_cell_type: HEK293 and second human cell line; purified proteins experimental_model: Human-cell siRNA plus recombinant cytochrome-b5/cofactor reconstitution limitations: Expression-dependent cellular contributions; no clinical iron or B2 supplementation test. exposure: mARC, CYB5B and CYB5A depletion; apo-CYB5 evidence_span: {"source_cache": "artifacts/molybdenum-research/23703616.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9034da6c790ca6e0c60dd765eec631ea2875c6caf65f6d15d59733bc5e0ee0ec", "start_char": 0, "end_char": 1596, "text_sha256": "9034da6c790ca6e0c60dd765eec631ea2875c6caf65f6d15d59733bc5e0ee0ec"} [mo-p23703616] The involvement of mitochondrial amidoxime reducing components 1 and 2 and mitochondrial cytochrome b5 in N-reductive metabolism in human cells. (2013). https://pubmed.ncbi.nlm.nih.gov/23703616/ DOI: 10.1074/jbc.m113.474916
Complete structured claim and evidence
Reduced human mARC1 generated nitric oxide from nitrite in the reconstituted electron-transfer chain.
Human mitochondrial amidoxime-reducing component 1 / MTARC1 → Nitrite / NO2(-) source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/24500710.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e4c2ab41c945d420266290d0241752039d7de2cb6223f9c64c7d0525c5688d9b", "start_char": 0, "end_char": 1585, "text_sha256": "e4c2ab41c945d420266290d0241752039d7de2cb6223f9c64c7d0525c5688d9b"}
experimental_model
Recombinant human mARC1/mARC2, active-site mutation, tungsten replacement and HEK expression
exposure
Reduced enzyme, nitrite, NADH/CYB5/CYB5R; pH 7.5 versus 6.5
limitations
Shows nitrite-reducing capacity; its share of NO production in normal people and response to mineral intake are not established.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens proteins and HEK cells
plain_language
mARC1 can also make NO from nitrite under suitable conditions.
primary_references
[mo-p24500710] Nitrite reductase and nitric-oxide synthase activity of the mitochondrial molybdopterin enzymes mARC1 and mARC2. (2014). https://pubmed.ncbi.nlm.nih.gov/24500710/ DOI: 10.1074/jbc.m114.555177
tissue_or_cell_type
Purified redox system and human cell model
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1028–1039
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human mARC1/mARC2, active-site mutation, tungsten replacement and HEK expression · source_derived_draft · unverified_draft
### mo-marc1-nitrite Reduced human mARC1 generated nitric oxide from nitrite in the reconstituted electron-transfer chain. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: mARC1 can also make NO from nitrite under suitable conditions. organism: Homo sapiens proteins and HEK cells tissue_or_cell_type: Purified redox system and human cell model experimental_model: Recombinant human mARC1/mARC2, active-site mutation, tungsten replacement and HEK expression limitations: Shows nitrite-reducing capacity; its share of NO production in normal people and response to mineral intake are not established. exposure: Reduced enzyme, nitrite, NADH/CYB5/CYB5R; pH 7.5 versus 6.5 evidence_span: {"source_cache": "artifacts/molybdenum-research/24500710.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e4c2ab41c945d420266290d0241752039d7de2cb6223f9c64c7d0525c5688d9b", "start_char": 0, "end_char": 1585, "text_sha256": "e4c2ab41c945d420266290d0241752039d7de2cb6223f9c64c7d0525c5688d9b"} [mo-p24500710] Nitrite reductase and nitric-oxide synthase activity of the mitochondrial molybdopterin enzymes mARC1 and mARC2. (2014). https://pubmed.ncbi.nlm.nih.gov/24500710/ DOI: 10.1074/jbc.m114.555177
Complete structured claim and evidence
Reduced human mARC2 also catalyzed nitrite-to-NO conversion.
Human mitochondrial amidoxime-reducing component 2 / MTARC2 → Nitrite / NO2(-) source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/24500710.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e4c2ab41c945d420266290d0241752039d7de2cb6223f9c64c7d0525c5688d9b", "start_char": 0, "end_char": 1585, "text_sha256": "e4c2ab41c945d420266290d0241752039d7de2cb6223f9c64c7d0525c5688d9b"}
experimental_model
Recombinant human mARC1/mARC2, active-site mutation, tungsten replacement and HEK expression
exposure
Reduced enzyme, nitrite, NADH/CYB5/CYB5R; pH 7.5 versus 6.5
limitations
Shows nitrite-reducing capacity; its share of NO production in normal people and response to mineral intake are not established.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens proteins and HEK cells
plain_language
mARC2 shares this conditional NO-forming capability.
primary_references
[mo-p24500710] Nitrite reductase and nitric-oxide synthase activity of the mitochondrial molybdopterin enzymes mARC1 and mARC2. (2014). https://pubmed.ncbi.nlm.nih.gov/24500710/ DOI: 10.1074/jbc.m114.555177
tissue_or_cell_type
Purified redox system and human cell model
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1041–1052
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human mARC1/mARC2, active-site mutation, tungsten replacement and HEK expression · source_derived_draft · unverified_draft
### mo-marc2-nitrite Reduced human mARC2 also catalyzed nitrite-to-NO conversion. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: mARC2 shares this conditional NO-forming capability. organism: Homo sapiens proteins and HEK cells tissue_or_cell_type: Purified redox system and human cell model experimental_model: Recombinant human mARC1/mARC2, active-site mutation, tungsten replacement and HEK expression limitations: Shows nitrite-reducing capacity; its share of NO production in normal people and response to mineral intake are not established. exposure: Reduced enzyme, nitrite, NADH/CYB5/CYB5R; pH 7.5 versus 6.5 evidence_span: {"source_cache": "artifacts/molybdenum-research/24500710.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e4c2ab41c945d420266290d0241752039d7de2cb6223f9c64c7d0525c5688d9b", "start_char": 0, "end_char": 1585, "text_sha256": "e4c2ab41c945d420266290d0241752039d7de2cb6223f9c64c7d0525c5688d9b"} [mo-p24500710] Nitrite reductase and nitric-oxide synthase activity of the mitochondrial molybdopterin enzymes mARC1 and mARC2. (2014). https://pubmed.ncbi.nlm.nih.gov/24500710/ DOI: 10.1074/jbc.m114.555177
Complete structured claim and evidence
Lowering assay pH from 7.5 to 6.5 increased the reported mARC NO-formation rate by nearly threefold.
Hydrogen ion → Human mitochondrial amidoxime-reducing component 1 / MTARC1 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/24500710.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e4c2ab41c945d420266290d0241752039d7de2cb6223f9c64c7d0525c5688d9b", "start_char": 0, "end_char": 1585, "text_sha256": "e4c2ab41c945d420266290d0241752039d7de2cb6223f9c64c7d0525c5688d9b"}
experimental_model
Recombinant human mARC1/mARC2, active-site mutation, tungsten replacement and HEK expression
exposure
Reduced enzyme, nitrite, NADH/CYB5/CYB5R; pH 7.5 versus 6.5
limitations
Shows nitrite-reducing capacity; its share of NO production in normal people and response to mineral intake are not established.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens proteins and HEK cells
plain_language
Acidity changed the reaction rate in this assay.
primary_references
[mo-p24500710] Nitrite reductase and nitric-oxide synthase activity of the mitochondrial molybdopterin enzymes mARC1 and mARC2. (2014). https://pubmed.ncbi.nlm.nih.gov/24500710/ DOI: 10.1074/jbc.m114.555177
tissue_or_cell_type
Purified redox system and human cell model
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1054–1065
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human mARC1/mARC2, active-site mutation, tungsten replacement and HEK expression · source_derived_draft · unverified_draft
### mo-marc-ph Lowering assay pH from 7.5 to 6.5 increased the reported mARC NO-formation rate by nearly threefold. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Acidity changed the reaction rate in this assay. organism: Homo sapiens proteins and HEK cells tissue_or_cell_type: Purified redox system and human cell model experimental_model: Recombinant human mARC1/mARC2, active-site mutation, tungsten replacement and HEK expression limitations: Shows nitrite-reducing capacity; its share of NO production in normal people and response to mineral intake are not established. exposure: Reduced enzyme, nitrite, NADH/CYB5/CYB5R; pH 7.5 versus 6.5 evidence_span: {"source_cache": "artifacts/molybdenum-research/24500710.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e4c2ab41c945d420266290d0241752039d7de2cb6223f9c64c7d0525c5688d9b", "start_char": 0, "end_char": 1585, "text_sha256": "e4c2ab41c945d420266290d0241752039d7de2cb6223f9c64c7d0525c5688d9b"} [mo-p24500710] Nitrite reductase and nitric-oxide synthase activity of the mitochondrial molybdopterin enzymes mARC1 and mARC2. (2014). https://pubmed.ncbi.nlm.nih.gov/24500710/ DOI: 10.1074/jbc.m114.555177
Complete structured claim and evidence
The C273A mARC1 variant abolished nitrite-dependent NO formation.
Human MTARC1 p.Cys273Ala → NO source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/24500710.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e4c2ab41c945d420266290d0241752039d7de2cb6223f9c64c7d0525c5688d9b", "start_char": 0, "end_char": 1585, "text_sha256": "e4c2ab41c945d420266290d0241752039d7de2cb6223f9c64c7d0525c5688d9b"}
experimental_model
Recombinant human mARC1/mARC2, active-site mutation, tungsten replacement and HEK expression
exposure
Reduced enzyme, nitrite, NADH/CYB5/CYB5R; pH 7.5 versus 6.5
limitations
Shows nitrite-reducing capacity; its share of NO production in normal people and response to mineral intake are not established.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens proteins and HEK cells
plain_language
The molybdenum-binding cysteine is critical for this reaction.
primary_references
[mo-p24500710] Nitrite reductase and nitric-oxide synthase activity of the mitochondrial molybdopterin enzymes mARC1 and mARC2. (2014). https://pubmed.ncbi.nlm.nih.gov/24500710/ DOI: 10.1074/jbc.m114.555177
tissue_or_cell_type
Purified redox system and human cell model
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1067–1078
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human mARC1/mARC2, active-site mutation, tungsten replacement and HEK expression · source_derived_draft · unverified_draft
### mo-marc-c273a The C273A mARC1 variant abolished nitrite-dependent NO formation. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The molybdenum-binding cysteine is critical for this reaction. organism: Homo sapiens proteins and HEK cells tissue_or_cell_type: Purified redox system and human cell model experimental_model: Recombinant human mARC1/mARC2, active-site mutation, tungsten replacement and HEK expression limitations: Shows nitrite-reducing capacity; its share of NO production in normal people and response to mineral intake are not established. exposure: Reduced enzyme, nitrite, NADH/CYB5/CYB5R; pH 7.5 versus 6.5 evidence_span: {"source_cache": "artifacts/molybdenum-research/24500710.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e4c2ab41c945d420266290d0241752039d7de2cb6223f9c64c7d0525c5688d9b", "start_char": 0, "end_char": 1585, "text_sha256": "e4c2ab41c945d420266290d0241752039d7de2cb6223f9c64c7d0525c5688d9b"} [mo-p24500710] Nitrite reductase and nitric-oxide synthase activity of the mitochondrial molybdopterin enzymes mARC1 and mARC2. (2014). https://pubmed.ncbi.nlm.nih.gov/24500710/ DOI: 10.1074/jbc.m114.555177
Complete structured claim and evidence
Replacing molybdenum with tungsten during recombinant mARC1 production abolished NO formation.
Tungsten-substituted recombinant human MTARC1 → NO source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/24500710.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e4c2ab41c945d420266290d0241752039d7de2cb6223f9c64c7d0525c5688d9b", "start_char": 0, "end_char": 1585, "text_sha256": "e4c2ab41c945d420266290d0241752039d7de2cb6223f9c64c7d0525c5688d9b"}
experimental_model
Recombinant human mARC1/mARC2, active-site mutation, tungsten replacement and HEK expression
exposure
Reduced enzyme, nitrite, NADH/CYB5/CYB5R; pH 7.5 versus 6.5
limitations
Shows nitrite-reducing capacity; its share of NO production in normal people and response to mineral intake are not established.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens proteins and HEK cells
plain_language
A chemically similar metal could not replace molybdenum in this reaction.
primary_references
[mo-p24500710] Nitrite reductase and nitric-oxide synthase activity of the mitochondrial molybdopterin enzymes mARC1 and mARC2. (2014). https://pubmed.ncbi.nlm.nih.gov/24500710/ DOI: 10.1074/jbc.m114.555177
tissue_or_cell_type
Purified redox system and human cell model
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1080–1091
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human mARC1/mARC2, active-site mutation, tungsten replacement and HEK expression · source_derived_draft · unverified_draft
### mo-marc-tungsten Replacing molybdenum with tungsten during recombinant mARC1 production abolished NO formation. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: A chemically similar metal could not replace molybdenum in this reaction. organism: Homo sapiens proteins and HEK cells tissue_or_cell_type: Purified redox system and human cell model experimental_model: Recombinant human mARC1/mARC2, active-site mutation, tungsten replacement and HEK expression limitations: Shows nitrite-reducing capacity; its share of NO production in normal people and response to mineral intake are not established. exposure: Reduced enzyme, nitrite, NADH/CYB5/CYB5R; pH 7.5 versus 6.5 evidence_span: {"source_cache": "artifacts/molybdenum-research/24500710.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e4c2ab41c945d420266290d0241752039d7de2cb6223f9c64c7d0525c5688d9b", "start_char": 0, "end_char": 1585, "text_sha256": "e4c2ab41c945d420266290d0241752039d7de2cb6223f9c64c7d0525c5688d9b"} [mo-p24500710] Nitrite reductase and nitric-oxide synthase activity of the mitochondrial molybdopterin enzymes mARC1 and mARC2. (2014). https://pubmed.ncbi.nlm.nih.gov/24500710/ DOI: 10.1074/jbc.m114.555177
Complete structured claim and evidence
Human SUOX reduced nitrite to NO at the molybdenum center, with steady-state turnover supported in a sulfite/cytochrome-c system.
Human sulfite oxidase / SUOX → Nitrite / NO2(-) source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/31167903.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9fb7f72eba7a1a254ae8e20991ee5d9ecbffc01de2a1dfc5879cf34bdbf98b45", "start_char": 0, "end_char": 962, "text_sha256": "9fb7f72eba7a1a254ae8e20991ee5d9ecbffc01de2a1dfc5879cf34bdbf98b45"}
experimental_model
Human SUOX kinetics, spectroscopy and electron-transfer variants
exposure
Nitrite with sulfite and cytochrome c
limitations
Biochemical capacity; contribution to human physiology requires separate evidence.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens protein
plain_language
SUOX can perform additional redox chemistry under the tested conditions.
primary_references
[mo-p31167903] Mechanism of nitrite-dependent NO synthesis by human sulfite oxidase. (2019). https://pubmed.ncbi.nlm.nih.gov/31167903/ DOI: 10.1042/bcj20190143
tissue_or_cell_type
Purified human sulfite oxidase
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1093–1104
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human SUOX kinetics, spectroscopy and electron-transfer variants · source_derived_draft · unverified_draft
### mo-suox-nitrite Human SUOX reduced nitrite to NO at the molybdenum center, with steady-state turnover supported in a sulfite/cytochrome-c system. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: SUOX can perform additional redox chemistry under the tested conditions. organism: Homo sapiens protein tissue_or_cell_type: Purified human sulfite oxidase experimental_model: Human SUOX kinetics, spectroscopy and electron-transfer variants limitations: Biochemical capacity; contribution to human physiology requires separate evidence. exposure: Nitrite with sulfite and cytochrome c evidence_span: {"source_cache": "artifacts/molybdenum-research/31167903.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9fb7f72eba7a1a254ae8e20991ee5d9ecbffc01de2a1dfc5879cf34bdbf98b45", "start_char": 0, "end_char": 962, "text_sha256": "9fb7f72eba7a1a254ae8e20991ee5d9ecbffc01de2a1dfc5879cf34bdbf98b45"} [mo-p31167903] Mechanism of nitrite-dependent NO synthesis by human sulfite oxidase. (2019). https://pubmed.ncbi.nlm.nih.gov/31167903/ DOI: 10.1042/bcj20190143
Complete structured claim and evidence
Electrochemical human SUOX nitrite reduction had a reported Km of 3.5 mM at pH 7; a heme-free variant behaved similarly in that system.
Human sulfite oxidase / SUOX → NO source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/41337830.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4cac9c7485dc06caae98c3fd1d54e64b47290a13869b96bfbee654dafdc2b20c", "start_char": 0, "end_char": 826, "text_sha256": "4cac9c7485dc06caae98c3fd1d54e64b47290a13869b96bfbee654dafdc2b20c"}
experimental_model
Electrochemically driven human SUOX nitrite-reductase assays
exposure
Benzyl-viologen mediator; pH-dependent assays
limitations
Artificial electron mediator and millimolar substrate affinity; physiological NO flux is not established.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens protein
plain_language
The laboratory reaction does not require every component used in the normal cellular pathway.
primary_references
[mo-p41337830] An electrochemical perspective on human sulfite oxidase as a potential nitrite reductase. (2026). https://pubmed.ncbi.nlm.nih.gov/41337830/ DOI: 10.1016/j.jinorgbio.2025.113159
tissue_or_cell_type
Purified enzyme on electrochemical system
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1106–1117
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Electrochemically driven human SUOX nitrite-reductase assays · source_derived_draft · unverified_draft
### mo-suox-nitrite-electrochemical Electrochemical human SUOX nitrite reduction had a reported Km of 3.5 mM at pH 7; a heme-free variant behaved similarly in that system. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The laboratory reaction does not require every component used in the normal cellular pathway. organism: Homo sapiens protein tissue_or_cell_type: Purified enzyme on electrochemical system experimental_model: Electrochemically driven human SUOX nitrite-reductase assays limitations: Artificial electron mediator and millimolar substrate affinity; physiological NO flux is not established. exposure: Benzyl-viologen mediator; pH-dependent assays evidence_span: {"source_cache": "artifacts/molybdenum-research/41337830.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4cac9c7485dc06caae98c3fd1d54e64b47290a13869b96bfbee654dafdc2b20c", "start_char": 0, "end_char": 826, "text_sha256": "4cac9c7485dc06caae98c3fd1d54e64b47290a13869b96bfbee654dafdc2b20c"} [mo-p41337830] An electrochemical perspective on human sulfite oxidase as a potential nitrite reductase. (2026). https://pubmed.ncbi.nlm.nih.gov/41337830/ DOI: 10.1016/j.jinorgbio.2025.113159
Complete structured claim and evidence
The prolonged-TPN case developed amino-acid intolerance with high plasma methionine, high urinary sulfite/thiosulfate and low urinary sulfate.
Molybdenum → Amino-acid intolerance during parenteral nutrition source_derived_draftungraded
Experimental context and source evidence
availability_state
nutrient_deficiency Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/6795919.publisher-abstract.txt", "locator": "Exact primary publisher abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d2838a46a598539818059c1a1f8295e283334afced15326a6b5ba1a6104cbfd7", "start_char": 0, "end_char": 1820, "text_sha256": "d2838a46a598539818059c1a1f8295e283334afced15326a6b5ba1a6104cbfd7"}
experimental_model
Single case during prolonged total parenteral nutrition
exposure
Prolonged parenteral nutrition followed by ammonium molybdate
limitations
Rare single case. The paper reports 300 micrograms/day ammonium molybdate, not 300 micrograms elemental molybdenum. Historical observation, not a general regimen.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
The sulfur-handling pathway stalled when molybdenum supply was inadequate.
primary_references
[mo-p6795919] Amino acid intolerance during prolonged total parenteral nutrition reversed by molybdate therapy. (1981). https://pubmed.ncbi.nlm.nih.gov/6795919/ DOI: 10.1093/ajcn/34.11.2551
tissue_or_cell_type
Systemic symptoms; plasma and urine
trigger_kind
nutrient_deficiency Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1119–1130
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Single case during prolonged total parenteral nutrition · source_derived_draft · unverified_draft
### mo-tpn-sulfur The prolonged-TPN case developed amino-acid intolerance with high plasma methionine, high urinary sulfite/thiosulfate and low urinary sulfate. Condition category: nutrient_deficiency nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The sulfur-handling pathway stalled when molybdenum supply was inadequate. organism: Homo sapiens tissue_or_cell_type: Systemic symptoms; plasma and urine experimental_model: Single case during prolonged total parenteral nutrition limitations: Rare single case. The paper reports 300 micrograms/day ammonium molybdate, not 300 micrograms elemental molybdenum. Historical observation, not a general regimen. exposure: Prolonged parenteral nutrition followed by ammonium molybdate evidence_span: {"source_cache": "artifacts/molybdenum-research/6795919.publisher-abstract.txt", "locator": "Exact primary publisher abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d2838a46a598539818059c1a1f8295e283334afced15326a6b5ba1a6104cbfd7", "start_char": 0, "end_char": 1820, "text_sha256": "d2838a46a598539818059c1a1f8295e283334afced15326a6b5ba1a6104cbfd7"} [mo-p6795919] Amino acid intolerance during prolonged total parenteral nutrition reversed by molybdate therapy. (1981). https://pubmed.ncbi.nlm.nih.gov/6795919/ DOI: 10.1093/ajcn/34.11.2551
Complete structured claim and evidence
The same patient had low serum urate with increased urinary hypoxanthine and xanthine.
Molybdenum → Serum urate concentration source_derived_draftungraded
Experimental context and source evidence
availability_state
nutrient_deficiency Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/6795919.publisher-abstract.txt", "locator": "Exact primary publisher abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d2838a46a598539818059c1a1f8295e283334afced15326a6b5ba1a6104cbfd7", "start_char": 0, "end_char": 1820, "text_sha256": "d2838a46a598539818059c1a1f8295e283334afced15326a6b5ba1a6104cbfd7"}
experimental_model
Single case during prolonged total parenteral nutrition
exposure
Prolonged parenteral nutrition followed by ammonium molybdate
limitations
Rare single case. The paper reports 300 micrograms/day ammonium molybdate, not 300 micrograms elemental molybdenum. Historical observation, not a general regimen.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
A second molybdenum-dependent pathway was also impaired.
primary_references
[mo-p6795919] Amino acid intolerance during prolonged total parenteral nutrition reversed by molybdate therapy. (1981). https://pubmed.ncbi.nlm.nih.gov/6795919/ DOI: 10.1093/ajcn/34.11.2551
tissue_or_cell_type
Systemic symptoms; plasma and urine
trigger_kind
nutrient_deficiency Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1132–1143
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Single case during prolonged total parenteral nutrition · source_derived_draft · unverified_draft
### mo-tpn-purines The same patient had low serum urate with increased urinary hypoxanthine and xanthine. Condition category: nutrient_deficiency nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: A second molybdenum-dependent pathway was also impaired. organism: Homo sapiens tissue_or_cell_type: Systemic symptoms; plasma and urine experimental_model: Single case during prolonged total parenteral nutrition limitations: Rare single case. The paper reports 300 micrograms/day ammonium molybdate, not 300 micrograms elemental molybdenum. Historical observation, not a general regimen. exposure: Prolonged parenteral nutrition followed by ammonium molybdate evidence_span: {"source_cache": "artifacts/molybdenum-research/6795919.publisher-abstract.txt", "locator": "Exact primary publisher abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d2838a46a598539818059c1a1f8295e283334afced15326a6b5ba1a6104cbfd7", "start_char": 0, "end_char": 1820, "text_sha256": "d2838a46a598539818059c1a1f8295e283334afced15326a6b5ba1a6104cbfd7"} [mo-p6795919] Amino acid intolerance during prolonged total parenteral nutrition reversed by molybdate therapy. (1981). https://pubmed.ncbi.nlm.nih.gov/6795919/ DOI: 10.1093/ajcn/34.11.2551
Complete structured claim and evidence
Ammonium molybdate improved the clinical condition, reversed the sulfur-handling defect and normalized urate production in the reported case.
Ammonium molybdate → Amino-acid intolerance during parenteral nutrition source_derived_draftungraded
Experimental context and source evidence
availability_state
nutrient_deficiency Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/6795919.publisher-abstract.txt", "locator": "Exact primary publisher abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d2838a46a598539818059c1a1f8295e283334afced15326a6b5ba1a6104cbfd7", "start_char": 0, "end_char": 1820, "text_sha256": "d2838a46a598539818059c1a1f8295e283334afced15326a6b5ba1a6104cbfd7"}
experimental_model
Single case during prolonged total parenteral nutrition
exposure
Prolonged parenteral nutrition followed by ammonium molybdate
limitations
Rare single case. The paper reports 300 micrograms/day ammonium molybdate, not 300 micrograms elemental molybdenum. Historical observation, not a general regimen.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
Replacement helped this documented acquired shortage.
primary_references
[mo-p6795919] Amino acid intolerance during prolonged total parenteral nutrition reversed by molybdate therapy. (1981). https://pubmed.ncbi.nlm.nih.gov/6795919/ DOI: 10.1093/ajcn/34.11.2551
tissue_or_cell_type
Systemic symptoms; plasma and urine
trigger_kind
nutrient_deficiency Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1145–1156
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Single case during prolonged total parenteral nutrition · source_derived_draft · unverified_draft
### mo-tpn-repletion Ammonium molybdate improved the clinical condition, reversed the sulfur-handling defect and normalized urate production in the reported case. Condition category: nutrient_deficiency nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Replacement helped this documented acquired shortage. organism: Homo sapiens tissue_or_cell_type: Systemic symptoms; plasma and urine experimental_model: Single case during prolonged total parenteral nutrition limitations: Rare single case. The paper reports 300 micrograms/day ammonium molybdate, not 300 micrograms elemental molybdenum. Historical observation, not a general regimen. exposure: Prolonged parenteral nutrition followed by ammonium molybdate evidence_span: {"source_cache": "artifacts/molybdenum-research/6795919.publisher-abstract.txt", "locator": "Exact primary publisher abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d2838a46a598539818059c1a1f8295e283334afced15326a6b5ba1a6104cbfd7", "start_char": 0, "end_char": 1820, "text_sha256": "d2838a46a598539818059c1a1f8295e283334afced15326a6b5ba1a6104cbfd7"} [mo-p6795919] Amino acid intolerance during prolonged total parenteral nutrition reversed by molybdate therapy. (1981). https://pubmed.ncbi.nlm.nih.gov/6795919/ DOI: 10.1093/ajcn/34.11.2551
Complete structured claim and evidence
MoCD-A and MoCD-B patients had elevated plasma/urinary S-sulfocysteine and xanthine, while urate stayed below reference ranges.
Molybdenum cofactor / Moco → Combined sulfur and purine biomarker pattern in Moco deficiency source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/35192225.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ab9083746ef775c196770d3f4d0208378f1796abf1d7056fe5b23f60421032d4", "start_char": 0, "end_char": 1812, "text_sha256": "ab9083746ef775c196770d3f4d0208378f1796abf1d7056fe5b23f60421032d4"}
experimental_model
Retrospective natural history in 58 patients; prospective biomarkers in 21 survivors
exposure
MoCD A:41; MoCD B:17
limitations
Severe inherited cofactor defects; not a prevalence study of ordinary nutritional deficiency or a validated population screening threshold.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
The combined pattern reflects failures in two cofactor-dependent pathways.
primary_references
[mo-p35192225] Molybdenum cofactor deficiency: A natural history. (2022). https://pubmed.ncbi.nlm.nih.gov/35192225/ DOI: 10.1002/jimd.12488
tissue_or_cell_type
Neurological course and plasma/urine
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1158–1169
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Retrospective natural history in 58 patients; prospective biomarkers in 21 survivors · source_derived_draft · unverified_draft
### mo-mocd-biomarkers MoCD-A and MoCD-B patients had elevated plasma/urinary S-sulfocysteine and xanthine, while urate stayed below reference ranges. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The combined pattern reflects failures in two cofactor-dependent pathways. organism: Homo sapiens tissue_or_cell_type: Neurological course and plasma/urine experimental_model: Retrospective natural history in 58 patients; prospective biomarkers in 21 survivors limitations: Severe inherited cofactor defects; not a prevalence study of ordinary nutritional deficiency or a validated population screening threshold. exposure: MoCD A:41; MoCD B:17 evidence_span: {"source_cache": "artifacts/molybdenum-research/35192225.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ab9083746ef775c196770d3f4d0208378f1796abf1d7056fe5b23f60421032d4", "start_char": 0, "end_char": 1812, "text_sha256": "ab9083746ef775c196770d3f4d0208378f1796abf1d7056fe5b23f60421032d4"} [mo-p35192225] Molybdenum cofactor deficiency: A natural history. (2022). https://pubmed.ncbi.nlm.nih.gov/35192225/ DOI: 10.1002/jimd.12488
Complete structured claim and evidence
Forty-nine of 58 patients had neonatal-onset symptoms; seizures, feeding difficulties and progressive neurological disability were common.
Molybdenum cofactor / Moco → Neurological outcome in molybdenum cofactor deficiency source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/35192225.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ab9083746ef775c196770d3f4d0208378f1796abf1d7056fe5b23f60421032d4", "start_char": 0, "end_char": 1812, "text_sha256": "ab9083746ef775c196770d3f4d0208378f1796abf1d7056fe5b23f60421032d4"}
experimental_model
Retrospective natural history in 58 patients; prospective biomarkers in 21 survivors
exposure
MoCD A:41; MoCD B:17
limitations
Severe inherited cofactor defects; not a prevalence study of ordinary nutritional deficiency or a validated population screening threshold.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
Severe inherited assembly failure has a very different course from a mildly low nutrient intake.
primary_references
[mo-p35192225] Molybdenum cofactor deficiency: A natural history. (2022). https://pubmed.ncbi.nlm.nih.gov/35192225/ DOI: 10.1002/jimd.12488
tissue_or_cell_type
Neurological course and plasma/urine
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1171–1182
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Retrospective natural history in 58 patients; prospective biomarkers in 21 survivors · source_derived_draft · unverified_draft
### mo-mocd-course Forty-nine of 58 patients had neonatal-onset symptoms; seizures, feeding difficulties and progressive neurological disability were common. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Severe inherited assembly failure has a very different course from a mildly low nutrient intake. organism: Homo sapiens tissue_or_cell_type: Neurological course and plasma/urine experimental_model: Retrospective natural history in 58 patients; prospective biomarkers in 21 survivors limitations: Severe inherited cofactor defects; not a prevalence study of ordinary nutritional deficiency or a validated population screening threshold. exposure: MoCD A:41; MoCD B:17 evidence_span: {"source_cache": "artifacts/molybdenum-research/35192225.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ab9083746ef775c196770d3f4d0208378f1796abf1d7056fe5b23f60421032d4", "start_char": 0, "end_char": 1812, "text_sha256": "ab9083746ef775c196770d3f4d0208378f1796abf1d7056fe5b23f60421032d4"} [mo-p35192225] Molybdenum cofactor deficiency: A natural history. (2022). https://pubmed.ncbi.nlm.nih.gov/35192225/ DOI: 10.1002/jimd.12488
Complete structured claim and evidence
Urinary S-sulfocysteine, xanthine and urate approached normal within two days in all 11 MoCD-A patients receiving cPMP; eight rapidly improved clinically.
Cyclic pyranopterin monophosphate / cPMP → Combined sulfur and purine biomarker pattern in Moco deficiency source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/26343839.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2ad559ea27a88eb8d55c30c517ca0ca53d01125912e43a330ed1290f37aff3ad", "start_char": 0, "end_char": 2265, "text_sha256": "2ad559ea27a88eb8d55c30c517ca0ca53d01125912e43a330ed1290f37aff3ad"}
experimental_model
Prospective compassionate-use observational cohort of 16 neonates
exposure
cPMP replacement in 11 type A and five type B patients
limitations
Nonrandomized rare-disease cohort. Precursor replacement bypasses a specific biosynthetic step; it is not ordinary mineral supplementation.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
Supplying the missing precursor can bypass the first assembly block.
primary_references
[mo-p26343839] Efficacy and safety of cyclic pyranopterin monophosphate substitution in severe molybdenum cofactor deficiency type A: a prospective cohort study. (2015). https://pubmed.ncbi.nlm.nih.gov/26343839/ DOI: 10.1016/s0140-6736(15)00124-5
tissue_or_cell_type
MoCD biochemical markers and neurological outcomes
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1184–1195
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Prospective compassionate-use observational cohort of 16 neonates · source_derived_draft · unverified_draft
### mo-cpmp-type-a Urinary S-sulfocysteine, xanthine and urate approached normal within two days in all 11 MoCD-A patients receiving cPMP; eight rapidly improved clinically. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Supplying the missing precursor can bypass the first assembly block. organism: Homo sapiens tissue_or_cell_type: MoCD biochemical markers and neurological outcomes experimental_model: Prospective compassionate-use observational cohort of 16 neonates limitations: Nonrandomized rare-disease cohort. Precursor replacement bypasses a specific biosynthetic step; it is not ordinary mineral supplementation. exposure: cPMP replacement in 11 type A and five type B patients evidence_span: {"source_cache": "artifacts/molybdenum-research/26343839.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2ad559ea27a88eb8d55c30c517ca0ca53d01125912e43a330ed1290f37aff3ad", "start_char": 0, "end_char": 2265, "text_sha256": "2ad559ea27a88eb8d55c30c517ca0ca53d01125912e43a330ed1290f37aff3ad"} [mo-p26343839] Efficacy and safety of cyclic pyranopterin monophosphate substitution in severe molybdenum cofactor deficiency type A: a prospective cohort study. (2015). https://pubmed.ncbi.nlm.nih.gov/26343839/ DOI: 10.1016/s0140-6736(15)00124-5
Complete structured claim and evidence
The five MoCD-B patients showed no biochemical or clinical response to cPMP.
Cyclic pyranopterin monophosphate / cPMP → Combined sulfur and purine biomarker pattern in Moco deficiency source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/26343839.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2ad559ea27a88eb8d55c30c517ca0ca53d01125912e43a330ed1290f37aff3ad", "start_char": 0, "end_char": 2265, "text_sha256": "2ad559ea27a88eb8d55c30c517ca0ca53d01125912e43a330ed1290f37aff3ad"}
experimental_model
Prospective compassionate-use observational cohort of 16 neonates
exposure
cPMP replacement in 11 type A and five type B patients
limitations
Nonrandomized rare-disease cohort. Precursor replacement bypasses a specific biosynthetic step; it is not ordinary mineral supplementation.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
Supplying an upstream precursor cannot repair a broken downstream step.
primary_references
[mo-p26343839] Efficacy and safety of cyclic pyranopterin monophosphate substitution in severe molybdenum cofactor deficiency type A: a prospective cohort study. (2015). https://pubmed.ncbi.nlm.nih.gov/26343839/ DOI: 10.1016/s0140-6736(15)00124-5
tissue_or_cell_type
MoCD biochemical markers and neurological outcomes
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1197–1208
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Prospective compassionate-use observational cohort of 16 neonates · source_derived_draft · unverified_draft
### mo-cpmp-type-b The five MoCD-B patients showed no biochemical or clinical response to cPMP. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Supplying an upstream precursor cannot repair a broken downstream step. organism: Homo sapiens tissue_or_cell_type: MoCD biochemical markers and neurological outcomes experimental_model: Prospective compassionate-use observational cohort of 16 neonates limitations: Nonrandomized rare-disease cohort. Precursor replacement bypasses a specific biosynthetic step; it is not ordinary mineral supplementation. exposure: cPMP replacement in 11 type A and five type B patients evidence_span: {"source_cache": "artifacts/molybdenum-research/26343839.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2ad559ea27a88eb8d55c30c517ca0ca53d01125912e43a330ed1290f37aff3ad", "start_char": 0, "end_char": 2265, "text_sha256": "2ad559ea27a88eb8d55c30c517ca0ca53d01125912e43a330ed1290f37aff3ad"} [mo-p26343839] Efficacy and safety of cyclic pyranopterin monophosphate substitution in severe molybdenum cofactor deficiency type A: a prospective cohort study. (2015). https://pubmed.ncbi.nlm.nih.gov/26343839/ DOI: 10.1016/s0140-6736(15)00124-5
Complete structured claim and evidence
Despite fosdenopterin within ten minutes of birth, the infant developed early seizures and retained motor impairment; seizures resolved and cognition was relatively spared.
Cyclic pyranopterin monophosphate / cPMP → Neurological outcome in molybdenum cofactor deficiency source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/40429556.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "25a9bcc9dc74084f82ec89ca2850ea25ee8ae156c6650d69ccd460d66d02e1d1", "start_char": 0, "end_char": 1369, "text_sha256": "25a9bcc9dc74084f82ec89ca2850ea25ee8ae156c6650d69ccd460d66d02e1d1"}
experimental_model
Prenatally diagnosed MoCD-A single case with immediate neonatal fosdenopterin
exposure
Delivery at 32 weeks 6 days; drug within 10 minutes of birth
limitations
One case. Residual injury suggests prenatal disease, but does not prove efficacy or safety of fetal treatment.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
Even rapid replacement may not undo injury that began before birth.
primary_references
[mo-p40429556] Early Neonatal Fosdenopterin Treatment for Molybdenum Cofactor Deficiency Type A: New Insights into Its Natural History and Potential Role for Fetal Therapy. (2025). https://pubmed.ncbi.nlm.nih.gov/40429556/ DOI: 10.3390/jcm14103561
tissue_or_cell_type
Fetal/neonatal brain and follow-up to 24 months
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1210–1221
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Prenatally diagnosed MoCD-A single case with immediate neonatal fosdenopterin · source_derived_draft · unverified_draft
### mo-cpmp-early-limit Despite fosdenopterin within ten minutes of birth, the infant developed early seizures and retained motor impairment; seizures resolved and cognition was relatively spared. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Even rapid replacement may not undo injury that began before birth. organism: Homo sapiens tissue_or_cell_type: Fetal/neonatal brain and follow-up to 24 months experimental_model: Prenatally diagnosed MoCD-A single case with immediate neonatal fosdenopterin limitations: One case. Residual injury suggests prenatal disease, but does not prove efficacy or safety of fetal treatment. exposure: Delivery at 32 weeks 6 days; drug within 10 minutes of birth evidence_span: {"source_cache": "artifacts/molybdenum-research/40429556.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "25a9bcc9dc74084f82ec89ca2850ea25ee8ae156c6650d69ccd460d66d02e1d1", "start_char": 0, "end_char": 1369, "text_sha256": "25a9bcc9dc74084f82ec89ca2850ea25ee8ae156c6650d69ccd460d66d02e1d1"} [mo-p40429556] Early Neonatal Fosdenopterin Treatment for Molybdenum Cofactor Deficiency Type A: New Insights into Its Natural History and Potential Role for Fetal Therapy. (2025). https://pubmed.ncbi.nlm.nih.gov/40429556/ DOI: 10.3390/jcm14103561
Complete structured claim and evidence
Three type I xanthinuria subjects had confirmed XDH gene defects; one tested nonsense variant lacked duodenal XDH protein despite preserved mRNA.
Human xanthine oxidoreductase / XDH → Classical type I xanthinuria phenotype source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/9153281.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "736b96f30570738a8aa1f55f33d1839eef8ce5911ce2c51b221db2e325517a0e", "start_char": 0, "end_char": 1243, "text_sha256": "736b96f30570738a8aa1f55f33d1839eef8ce5911ce2c51b221db2e325517a0e"}
experimental_model
Genetic analysis of four classical-xanthinuria subjects
exposure
XDH nonsense and frameshift variants
limitations
Specific XDH deficiency, distinct from loss of all Moco synthesis or the combined XDH/AOX1 deficiency of MOCOS defects.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
An enzyme-specific genetic defect should not be labeled a shortage of the mineral.
primary_references
[mo-p9153281] Identification of two mutations in human xanthine dehydrogenase gene responsible for classical type I xanthinuria. (1997). https://pubmed.ncbi.nlm.nih.gov/9153281/ DOI: 10.1172/jci119421
tissue_or_cell_type
Duodenal mucosa and genetics
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1223–1234
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Genetic analysis of four classical-xanthinuria subjects · source_derived_draft · unverified_draft
### mo-xdh-type-i Three type I xanthinuria subjects had confirmed XDH gene defects; one tested nonsense variant lacked duodenal XDH protein despite preserved mRNA. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: An enzyme-specific genetic defect should not be labeled a shortage of the mineral. organism: Homo sapiens tissue_or_cell_type: Duodenal mucosa and genetics experimental_model: Genetic analysis of four classical-xanthinuria subjects limitations: Specific XDH deficiency, distinct from loss of all Moco synthesis or the combined XDH/AOX1 deficiency of MOCOS defects. exposure: XDH nonsense and frameshift variants evidence_span: {"source_cache": "artifacts/molybdenum-research/9153281.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "736b96f30570738a8aa1f55f33d1839eef8ce5911ce2c51b221db2e325517a0e", "start_char": 0, "end_char": 1243, "text_sha256": "736b96f30570738a8aa1f55f33d1839eef8ce5911ce2c51b221db2e325517a0e"} [mo-p9153281] Identification of two mutations in human xanthine dehydrogenase gene responsible for classical type I xanthinuria. (1997). https://pubmed.ncbi.nlm.nih.gov/9153281/ DOI: 10.1172/jci119421
Complete structured claim and evidence
Sulfite reacted stoichiometrically with cystine to form SSC; reduced cysteine did not form SSC in the same assay.
Sulfite / SO3(2-) → S-Sulfocysteine source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/29106383.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d7cfb311498ba2a88e3fc04be988dcffda740bbd1d93ada686cabf801861cf2a", "start_char": 14310, "end_char": 15490, "text_sha256": "9a181fcee8488d6f7513a0fa1759320721a8663e58658ef9344c1354716e3284"}
experimental_model
Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice
exposure
SSC/sulfite exposure; receptor/calcium/calpain inhibition
limitations
Mechanistic model evidence. Mouse drug rescue does not establish human treatment efficacy; sulfite also has SSC-independent toxicity.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Mus musculus neurons and mice; chemical reaction assays
plain_language
The oxidized and reduced forms of cysteine behave differently.
primary_references
[mo-p29106383] S-sulfocysteine/NMDA receptor-dependent signaling underlies neurodegeneration in molybdenum cofactor deficiency. (2017). https://pubmed.ncbi.nlm.nih.gov/29106383/ DOI: 10.1172/jci89885
tissue_or_cell_type
Neuronal receptors, intracellular calcium and inhibitory synapses
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1236–1247
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice · source_derived_draft · unverified_draft
### mo-ssc-formation Sulfite reacted stoichiometrically with cystine to form SSC; reduced cysteine did not form SSC in the same assay. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The oxidized and reduced forms of cysteine behave differently. organism: Mus musculus neurons and mice; chemical reaction assays tissue_or_cell_type: Neuronal receptors, intracellular calcium and inhibitory synapses experimental_model: Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice limitations: Mechanistic model evidence. Mouse drug rescue does not establish human treatment efficacy; sulfite also has SSC-independent toxicity. exposure: SSC/sulfite exposure; receptor/calcium/calpain inhibition evidence_span: {"source_cache": "artifacts/molybdenum-research/29106383.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d7cfb311498ba2a88e3fc04be988dcffda740bbd1d93ada686cabf801861cf2a", "start_char": 14310, "end_char": 15490, "text_sha256": "9a181fcee8488d6f7513a0fa1759320721a8663e58658ef9344c1354716e3284"} [mo-p29106383] S-sulfocysteine/NMDA receptor-dependent signaling underlies neurodegeneration in molybdenum cofactor deficiency. (2017). https://pubmed.ncbi.nlm.nih.gov/29106383/ DOI: 10.1172/jci89885
Complete structured claim and evidence
SSC acted as an NMDA-receptor agonist in primary murine neurons.
S-Sulfocysteine → NMDA-type glutamate receptors source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/29106383.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c", "start_char": 0, "end_char": 1472, "text_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c"}
experimental_model
Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice
exposure
SSC/sulfite exposure; receptor/calcium/calpain inhibition
limitations
Mechanistic model evidence. Mouse drug rescue does not establish human treatment efficacy; sulfite also has SSC-independent toxicity.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Mus musculus neurons and mice; chemical reaction assays
plain_language
A sulfur metabolite can imitate an excitatory neurotransmitter.
primary_references
[mo-p29106383] S-sulfocysteine/NMDA receptor-dependent signaling underlies neurodegeneration in molybdenum cofactor deficiency. (2017). https://pubmed.ncbi.nlm.nih.gov/29106383/ DOI: 10.1172/jci89885
tissue_or_cell_type
Neuronal receptors, intracellular calcium and inhibitory synapses
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1249–1260
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice · source_derived_draft · unverified_draft
### mo-ssc-nmda SSC acted as an NMDA-receptor agonist in primary murine neurons. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: A sulfur metabolite can imitate an excitatory neurotransmitter. organism: Mus musculus neurons and mice; chemical reaction assays tissue_or_cell_type: Neuronal receptors, intracellular calcium and inhibitory synapses experimental_model: Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice limitations: Mechanistic model evidence. Mouse drug rescue does not establish human treatment efficacy; sulfite also has SSC-independent toxicity. exposure: SSC/sulfite exposure; receptor/calcium/calpain inhibition evidence_span: {"source_cache": "artifacts/molybdenum-research/29106383.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c", "start_char": 0, "end_char": 1472, "text_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c"} [mo-p29106383] S-sulfocysteine/NMDA receptor-dependent signaling underlies neurodegeneration in molybdenum cofactor deficiency. (2017). https://pubmed.ncbi.nlm.nih.gov/29106383/ DOI: 10.1172/jci89885
Complete structured claim and evidence
Combined NMDA- and AMPA-receptor blockade almost completely suppressed SSC-evoked currents, supporting SSC agonism at both receptor classes.
S-Sulfocysteine → AMPA-type glutamate receptors source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/29106383.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d7cfb311498ba2a88e3fc04be988dcffda740bbd1d93ada686cabf801861cf2a", "start_char": 16686, "end_char": 17024, "text_sha256": "bc275c8c18044e88885db4ff2c7ebbca4376b6e4c1b7b88b66385a33c7775b5b"}
experimental_model
Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice
exposure
SSC/sulfite exposure; receptor/calcium/calpain inhibition
limitations
Mechanistic model evidence. Mouse drug rescue does not establish human treatment efficacy; sulfite also has SSC-independent toxicity.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Mus musculus neurons and mice; chemical reaction assays
plain_language
More than one excitatory receptor contributed to the electrical response.
primary_references
[mo-p29106383] S-sulfocysteine/NMDA receptor-dependent signaling underlies neurodegeneration in molybdenum cofactor deficiency. (2017). https://pubmed.ncbi.nlm.nih.gov/29106383/ DOI: 10.1172/jci89885
tissue_or_cell_type
Neuronal receptors, intracellular calcium and inhibitory synapses
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1262–1273
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice · source_derived_draft · unverified_draft
### mo-ssc-ampa Combined NMDA- and AMPA-receptor blockade almost completely suppressed SSC-evoked currents, supporting SSC agonism at both receptor classes. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: More than one excitatory receptor contributed to the electrical response. organism: Mus musculus neurons and mice; chemical reaction assays tissue_or_cell_type: Neuronal receptors, intracellular calcium and inhibitory synapses experimental_model: Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice limitations: Mechanistic model evidence. Mouse drug rescue does not establish human treatment efficacy; sulfite also has SSC-independent toxicity. exposure: SSC/sulfite exposure; receptor/calcium/calpain inhibition evidence_span: {"source_cache": "artifacts/molybdenum-research/29106383.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d7cfb311498ba2a88e3fc04be988dcffda740bbd1d93ada686cabf801861cf2a", "start_char": 16686, "end_char": 17024, "text_sha256": "bc275c8c18044e88885db4ff2c7ebbca4376b6e4c1b7b88b66385a33c7775b5b"} [mo-p29106383] S-sulfocysteine/NMDA receptor-dependent signaling underlies neurodegeneration in molybdenum cofactor deficiency. (2017). https://pubmed.ncbi.nlm.nih.gov/29106383/ DOI: 10.1172/jci89885
Complete structured claim and evidence
SSC receptor activation caused neuronal calcium influx.
S-Sulfocysteine → Neuronal calcium influx source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/29106383.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c", "start_char": 0, "end_char": 1472, "text_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c"}
experimental_model
Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice
exposure
SSC/sulfite exposure; receptor/calcium/calpain inhibition
limitations
Mechanistic model evidence. Mouse drug rescue does not establish human treatment efficacy; sulfite also has SSC-independent toxicity.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Mus musculus neurons and mice; chemical reaction assays
plain_language
Receptor activation opens the way for calcium to enter.
primary_references
[mo-p29106383] S-sulfocysteine/NMDA receptor-dependent signaling underlies neurodegeneration in molybdenum cofactor deficiency. (2017). https://pubmed.ncbi.nlm.nih.gov/29106383/ DOI: 10.1172/jci89885
tissue_or_cell_type
Neuronal receptors, intracellular calcium and inhibitory synapses
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1275–1286
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice · source_derived_draft · unverified_draft
### mo-ssc-calcium SSC receptor activation caused neuronal calcium influx. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Receptor activation opens the way for calcium to enter. organism: Mus musculus neurons and mice; chemical reaction assays tissue_or_cell_type: Neuronal receptors, intracellular calcium and inhibitory synapses experimental_model: Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice limitations: Mechanistic model evidence. Mouse drug rescue does not establish human treatment efficacy; sulfite also has SSC-independent toxicity. exposure: SSC/sulfite exposure; receptor/calcium/calpain inhibition evidence_span: {"source_cache": "artifacts/molybdenum-research/29106383.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c", "start_char": 0, "end_char": 1472, "text_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c"} [mo-p29106383] S-sulfocysteine/NMDA receptor-dependent signaling underlies neurodegeneration in molybdenum cofactor deficiency. (2017). https://pubmed.ncbi.nlm.nih.gov/29106383/ DOI: 10.1172/jci89885
Complete structured claim and evidence
SSC exposure activated calpain; blockade of calcium entry or calpain prevented the measured excitotoxicity.
S-Sulfocysteine → Calcium-dependent calpain proteases source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/29106383.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c", "start_char": 0, "end_char": 1472, "text_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c"}
experimental_model
Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice
exposure
SSC/sulfite exposure; receptor/calcium/calpain inhibition
limitations
Mechanistic model evidence. Mouse drug rescue does not establish human treatment efficacy; sulfite also has SSC-independent toxicity.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Mus musculus neurons and mice; chemical reaction assays
plain_language
Calcium-dependent proteases connect the signal to cellular damage.
primary_references
[mo-p29106383] S-sulfocysteine/NMDA receptor-dependent signaling underlies neurodegeneration in molybdenum cofactor deficiency. (2017). https://pubmed.ncbi.nlm.nih.gov/29106383/ DOI: 10.1172/jci89885
tissue_or_cell_type
Neuronal receptors, intracellular calcium and inhibitory synapses
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1288–1299
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice · source_derived_draft · unverified_draft
### mo-ssc-calpain SSC exposure activated calpain; blockade of calcium entry or calpain prevented the measured excitotoxicity. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Calcium-dependent proteases connect the signal to cellular damage. organism: Mus musculus neurons and mice; chemical reaction assays tissue_or_cell_type: Neuronal receptors, intracellular calcium and inhibitory synapses experimental_model: Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice limitations: Mechanistic model evidence. Mouse drug rescue does not establish human treatment efficacy; sulfite also has SSC-independent toxicity. exposure: SSC/sulfite exposure; receptor/calcium/calpain inhibition evidence_span: {"source_cache": "artifacts/molybdenum-research/29106383.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c", "start_char": 0, "end_char": 1472, "text_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c"} [mo-p29106383] S-sulfocysteine/NMDA receptor-dependent signaling underlies neurodegeneration in molybdenum cofactor deficiency. (2017). https://pubmed.ncbi.nlm.nih.gov/29106383/ DOI: 10.1172/jci89885
Complete structured claim and evidence
Calpain-dependent gephyrin degradation exacerbated SSC-mediated excitotoxicity in the neuronal experiments.
Calcium-dependent calpain proteases → Mouse gephyrin / Gphn source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/29106383.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c", "start_char": 0, "end_char": 1472, "text_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c"}
experimental_model
Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice
exposure
SSC/sulfite exposure; receptor/calcium/calpain inhibition
limitations
Mechanistic model evidence. Mouse drug rescue does not establish human treatment efficacy; sulfite also has SSC-independent toxicity.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Mus musculus neurons and mice; chemical reaction assays
plain_language
A protein that anchors inhibitory signaling was broken down.
primary_references
[mo-p29106383] S-sulfocysteine/NMDA receptor-dependent signaling underlies neurodegeneration in molybdenum cofactor deficiency. (2017). https://pubmed.ncbi.nlm.nih.gov/29106383/ DOI: 10.1172/jci89885
tissue_or_cell_type
Neuronal receptors, intracellular calcium and inhibitory synapses
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1301–1312
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice · source_derived_draft · unverified_draft
### mo-calpain-gephyrin Calpain-dependent gephyrin degradation exacerbated SSC-mediated excitotoxicity in the neuronal experiments. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: A protein that anchors inhibitory signaling was broken down. organism: Mus musculus neurons and mice; chemical reaction assays tissue_or_cell_type: Neuronal receptors, intracellular calcium and inhibitory synapses experimental_model: Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice limitations: Mechanistic model evidence. Mouse drug rescue does not establish human treatment efficacy; sulfite also has SSC-independent toxicity. exposure: SSC/sulfite exposure; receptor/calcium/calpain inhibition evidence_span: {"source_cache": "artifacts/molybdenum-research/29106383.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c", "start_char": 0, "end_char": 1472, "text_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c"} [mo-p29106383] S-sulfocysteine/NMDA receptor-dependent signaling underlies neurodegeneration in molybdenum cofactor deficiency. (2017). https://pubmed.ncbi.nlm.nih.gov/29106383/ DOI: 10.1172/jci89885
Complete structured claim and evidence
SSC-associated gephyrin degradation promoted loss of GABAergic synapses.
Mouse gephyrin / Gphn → GABAergic synapse retention source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/29106383.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c", "start_char": 0, "end_char": 1472, "text_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c"}
experimental_model
Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice
exposure
SSC/sulfite exposure; receptor/calcium/calpain inhibition
limitations
Mechanistic model evidence. Mouse drug rescue does not establish human treatment efficacy; sulfite also has SSC-independent toxicity.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Mus musculus neurons and mice; chemical reaction assays
plain_language
Losing inhibitory synapses can worsen the imbalance toward excitation.
primary_references
[mo-p29106383] S-sulfocysteine/NMDA receptor-dependent signaling underlies neurodegeneration in molybdenum cofactor deficiency. (2017). https://pubmed.ncbi.nlm.nih.gov/29106383/ DOI: 10.1172/jci89885
tissue_or_cell_type
Neuronal receptors, intracellular calcium and inhibitory synapses
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1314–1325
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice · source_derived_draft · unverified_draft
### mo-gephyrin-synapses SSC-associated gephyrin degradation promoted loss of GABAergic synapses. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Losing inhibitory synapses can worsen the imbalance toward excitation. organism: Mus musculus neurons and mice; chemical reaction assays tissue_or_cell_type: Neuronal receptors, intracellular calcium and inhibitory synapses experimental_model: Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice limitations: Mechanistic model evidence. Mouse drug rescue does not establish human treatment efficacy; sulfite also has SSC-independent toxicity. exposure: SSC/sulfite exposure; receptor/calcium/calpain inhibition evidence_span: {"source_cache": "artifacts/molybdenum-research/29106383.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c", "start_char": 0, "end_char": 1472, "text_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c"} [mo-p29106383] S-sulfocysteine/NMDA receptor-dependent signaling underlies neurodegeneration in molybdenum cofactor deficiency. (2017). https://pubmed.ncbi.nlm.nih.gov/29106383/ DOI: 10.1172/jci89885
Complete structured claim and evidence
Blocking NMDA receptors, calcium influx or calpain abolished SSC and glutamate toxicity in primary murine neurons.
NMDA-type glutamate receptors → Neuronal excitotoxic cell death source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/29106383.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c", "start_char": 0, "end_char": 1472, "text_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c"}
experimental_model
Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice
exposure
SSC/sulfite exposure; receptor/calcium/calpain inhibition
limitations
Mechanistic model evidence. Mouse drug rescue does not establish human treatment efficacy; sulfite also has SSC-independent toxicity.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Mus musculus neurons and mice; chemical reaction assays
plain_language
Interrupting several points in the chain prevented damage in this model.
primary_references
[mo-p29106383] S-sulfocysteine/NMDA receptor-dependent signaling underlies neurodegeneration in molybdenum cofactor deficiency. (2017). https://pubmed.ncbi.nlm.nih.gov/29106383/ DOI: 10.1172/jci89885
tissue_or_cell_type
Neuronal receptors, intracellular calcium and inhibitory synapses
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1327–1338
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice · source_derived_draft · unverified_draft
### mo-ssc-blockade Blocking NMDA receptors, calcium influx or calpain abolished SSC and glutamate toxicity in primary murine neurons. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Interrupting several points in the chain prevented damage in this model. organism: Mus musculus neurons and mice; chemical reaction assays tissue_or_cell_type: Neuronal receptors, intracellular calcium and inhibitory synapses experimental_model: Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice limitations: Mechanistic model evidence. Mouse drug rescue does not establish human treatment efficacy; sulfite also has SSC-independent toxicity. exposure: SSC/sulfite exposure; receptor/calcium/calpain inhibition evidence_span: {"source_cache": "artifacts/molybdenum-research/29106383.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c", "start_char": 0, "end_char": 1472, "text_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c"} [mo-p29106383] S-sulfocysteine/NMDA receptor-dependent signaling underlies neurodegeneration in molybdenum cofactor deficiency. (2017). https://pubmed.ncbi.nlm.nih.gov/29106383/ DOI: 10.1172/jci89885
Complete structured claim and evidence
Sulfite retained cytotoxicity in cystine-free medium, and MK801 failed to rescue that component.
Sulfite / SO3(2-) → S-Sulfocysteine-independent sulfite cytotoxicity source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/29106383.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d7cfb311498ba2a88e3fc04be988dcffda740bbd1d93ada686cabf801861cf2a", "start_char": 14836, "end_char": 15490, "text_sha256": "e325c707b167b422f3b1aa7650a7dfdf7b9fca124d93bd15827b2ebbbd1ea8da"}
experimental_model
Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice
exposure
SSC/sulfite exposure; receptor/calcium/calpain inhibition
limitations
Mechanistic model evidence. Mouse drug rescue does not establish human treatment efficacy; sulfite also has SSC-independent toxicity.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Mus musculus neurons and mice; chemical reaction assays
plain_language
Blocking the SSC receptor pathway does not explain or prevent every sulfite effect.
primary_references
[mo-p29106383] S-sulfocysteine/NMDA receptor-dependent signaling underlies neurodegeneration in molybdenum cofactor deficiency. (2017). https://pubmed.ncbi.nlm.nih.gov/29106383/ DOI: 10.1172/jci89885
tissue_or_cell_type
Neuronal receptors, intracellular calcium and inhibitory synapses
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1340–1351
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice · source_derived_draft · unverified_draft
### mo-sulfite-independent Sulfite retained cytotoxicity in cystine-free medium, and MK801 failed to rescue that component. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Blocking the SSC receptor pathway does not explain or prevent every sulfite effect. organism: Mus musculus neurons and mice; chemical reaction assays tissue_or_cell_type: Neuronal receptors, intracellular calcium and inhibitory synapses experimental_model: Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice limitations: Mechanistic model evidence. Mouse drug rescue does not establish human treatment efficacy; sulfite also has SSC-independent toxicity. exposure: SSC/sulfite exposure; receptor/calcium/calpain inhibition evidence_span: {"source_cache": "artifacts/molybdenum-research/29106383.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d7cfb311498ba2a88e3fc04be988dcffda740bbd1d93ada686cabf801861cf2a", "start_char": 14836, "end_char": 15490, "text_sha256": "e325c707b167b422f3b1aa7650a7dfdf7b9fca124d93bd15827b2ebbbd1ea8da"} [mo-p29106383] S-sulfocysteine/NMDA receptor-dependent signaling underlies neurodegeneration in molybdenum cofactor deficiency. (2017). https://pubmed.ncbi.nlm.nih.gov/29106383/ DOI: 10.1172/jci89885
Complete structured claim and evidence
Memantine protected against symptom manifestation in a tungstate-induced MoCD mouse model.
Memantine → Neurological outcome in molybdenum cofactor deficiency source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/29106383.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c", "start_char": 0, "end_char": 1472, "text_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c"}
experimental_model
Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice
exposure
SSC/sulfite exposure; receptor/calcium/calpain inhibition
limitations
Mechanistic model evidence. Mouse drug rescue does not establish human treatment efficacy; sulfite also has SSC-independent toxicity.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Mus musculus neurons and mice; chemical reaction assays
plain_language
An NMDA blocker helped in this induced mouse model.
primary_references
[mo-p29106383] S-sulfocysteine/NMDA receptor-dependent signaling underlies neurodegeneration in molybdenum cofactor deficiency. (2017). https://pubmed.ncbi.nlm.nih.gov/29106383/ DOI: 10.1172/jci89885
tissue_or_cell_type
Neuronal receptors, intracellular calcium and inhibitory synapses
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1353–1364
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice · source_derived_draft · unverified_draft
### mo-memantine-mouse Memantine protected against symptom manifestation in a tungstate-induced MoCD mouse model. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: An NMDA blocker helped in this induced mouse model. organism: Mus musculus neurons and mice; chemical reaction assays tissue_or_cell_type: Neuronal receptors, intracellular calcium and inhibitory synapses experimental_model: Primary murine neurons, chemical reaction assays and tungstate-induced MoCD mice limitations: Mechanistic model evidence. Mouse drug rescue does not establish human treatment efficacy; sulfite also has SSC-independent toxicity. exposure: SSC/sulfite exposure; receptor/calcium/calpain inhibition evidence_span: {"source_cache": "artifacts/molybdenum-research/29106383.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c", "start_char": 0, "end_char": 1472, "text_sha256": "34a677525363617e386b99e8ada3d049bc6147617c92764ca09caf1cae8efa1c"} [mo-p29106383] S-sulfocysteine/NMDA receptor-dependent signaling underlies neurodegeneration in molybdenum cofactor deficiency. (2017). https://pubmed.ncbi.nlm.nih.gov/29106383/ DOI: 10.1172/jci89885
Complete structured claim and evidence
Sulfite inhibited rat-brain glutamate dehydrogenase and reduced glutamate-supported NADH production.
Sulfite / SO3(2-) → Rat glutamate dehydrogenase / Glud1 source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/15273247.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d2f73a9ca41e4d51b85d3a66ada08511055ce6ff7462beb0e7eaf21aadf37279", "start_char": 0, "end_char": 1606, "text_sha256": "d2f73a9ca41e4d51b85d3a66ada08511055ce6ff7462beb0e7eaf21aadf37279"}
experimental_model
Rat brain mitochondria/extracts, purified enzyme and Neuro-2a/PC12 cells
exposure
Micromolar sulfite exposure
limitations
Experimental substrate dependence; not a measurement of these effects in people with ordinary low molybdenum intake.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Rattus norvegicus tissue; rodent cell lines
plain_language
A sulfur-metabolism disturbance can interrupt a separate fuel-processing enzyme.
primary_references
[mo-p15273247] A mechanism of sulfite neurotoxicity: direct inhibition of glutamate dehydrogenase. (2004). https://pubmed.ncbi.nlm.nih.gov/15273247/ DOI: 10.1074/jbc.m402759200
tissue_or_cell_type
Mitochondrial glutamate oxidation
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1366–1377
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Rat brain mitochondria/extracts, purified enzyme and Neuro-2a/PC12 cells · source_derived_draft · unverified_draft
### mo-sulfite-gdh Sulfite inhibited rat-brain glutamate dehydrogenase and reduced glutamate-supported NADH production. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: A sulfur-metabolism disturbance can interrupt a separate fuel-processing enzyme. organism: Rattus norvegicus tissue; rodent cell lines tissue_or_cell_type: Mitochondrial glutamate oxidation experimental_model: Rat brain mitochondria/extracts, purified enzyme and Neuro-2a/PC12 cells limitations: Experimental substrate dependence; not a measurement of these effects in people with ordinary low molybdenum intake. exposure: Micromolar sulfite exposure evidence_span: {"source_cache": "artifacts/molybdenum-research/15273247.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d2f73a9ca41e4d51b85d3a66ada08511055ce6ff7462beb0e7eaf21aadf37279", "start_char": 0, "end_char": 1606, "text_sha256": "d2f73a9ca41e4d51b85d3a66ada08511055ce6ff7462beb0e7eaf21aadf37279"} [mo-p15273247] A mechanism of sulfite neurotoxicity: direct inhibition of glutamate dehydrogenase. (2004). https://pubmed.ncbi.nlm.nih.gov/15273247/ DOI: 10.1074/jbc.m402759200
Complete structured claim and evidence
Sulfite reduced glutamate-driven mitochondrial membrane potential and ATP synthesis, while malate- and succinate-supported membrane potential was not affected.
Sulfite / SO3(2-) → Mitochondrial ATP production source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/15273247.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d2f73a9ca41e4d51b85d3a66ada08511055ce6ff7462beb0e7eaf21aadf37279", "start_char": 0, "end_char": 1606, "text_sha256": "d2f73a9ca41e4d51b85d3a66ada08511055ce6ff7462beb0e7eaf21aadf37279"}
experimental_model
Rat brain mitochondria/extracts, purified enzyme and Neuro-2a/PC12 cells
exposure
Micromolar sulfite exposure
limitations
Experimental substrate dependence; not a measurement of these effects in people with ordinary low molybdenum intake.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Rattus norvegicus tissue; rodent cell lines
plain_language
The effect depended on which fuel route supplied the mitochondria.
primary_references
[mo-p15273247] A mechanism of sulfite neurotoxicity: direct inhibition of glutamate dehydrogenase. (2004). https://pubmed.ncbi.nlm.nih.gov/15273247/ DOI: 10.1074/jbc.m402759200
tissue_or_cell_type
Mitochondrial glutamate oxidation
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1379–1390
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Rat brain mitochondria/extracts, purified enzyme and Neuro-2a/PC12 cells · source_derived_draft · unverified_draft
### mo-sulfite-atp Sulfite reduced glutamate-driven mitochondrial membrane potential and ATP synthesis, while malate- and succinate-supported membrane potential was not affected. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The effect depended on which fuel route supplied the mitochondria. organism: Rattus norvegicus tissue; rodent cell lines tissue_or_cell_type: Mitochondrial glutamate oxidation experimental_model: Rat brain mitochondria/extracts, purified enzyme and Neuro-2a/PC12 cells limitations: Experimental substrate dependence; not a measurement of these effects in people with ordinary low molybdenum intake. exposure: Micromolar sulfite exposure evidence_span: {"source_cache": "artifacts/molybdenum-research/15273247.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d2f73a9ca41e4d51b85d3a66ada08511055ce6ff7462beb0e7eaf21aadf37279", "start_char": 0, "end_char": 1606, "text_sha256": "d2f73a9ca41e4d51b85d3a66ada08511055ce6ff7462beb0e7eaf21aadf37279"} [mo-p15273247] A mechanism of sulfite neurotoxicity: direct inhibition of glutamate dehydrogenase. (2004). https://pubmed.ncbi.nlm.nih.gov/15273247/ DOI: 10.1074/jbc.m402759200
Complete structured claim and evidence
One-hour sulfite exposure reduced glutamate uptake in cortical slices; thiosulfate did not.
Sulfite / SO3(2-) → Rat cortical glutamate uptake source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/25777939.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1768480178724867d4c7a98f723cfd1a0010f7973eae4a4baea3d1261a06fdd2", "start_char": 0, "end_char": 2017, "text_sha256": "1768480178724867d4c7a98f723cfd1a0010f7973eae4a4baea3d1261a06fdd2"}
experimental_model
Sulfite/thiosulfate incubation of rat cortical slices and cell-free GSSG
exposure
One- versus three-hour incubations; 10 micromolar sulfite redox observations
limitations
Concentration, duration and preparation matter; GPx activity is not evidence of selenium depletion.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Rattus norvegicus; cell-free comparison
plain_language
Less uptake may prolong extracellular excitatory signaling.
primary_references
[mo-p25777939] In vitro evidence that sulfite impairs glutamatergic neurotransmission and inhibits glutathione metabolism-related enzymes in rat cerebral cortex. (2015). https://pubmed.ncbi.nlm.nih.gov/25777939/ DOI: 10.1016/j.ijdevneu.2015.03.005
tissue_or_cell_type
Cerebral cortex
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1392–1403
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Sulfite/thiosulfate incubation of rat cortical slices and cell-free GSSG · source_derived_draft · unverified_draft
### mo-sulfite-glutamate-uptake One-hour sulfite exposure reduced glutamate uptake in cortical slices; thiosulfate did not. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Less uptake may prolong extracellular excitatory signaling. organism: Rattus norvegicus; cell-free comparison tissue_or_cell_type: Cerebral cortex experimental_model: Sulfite/thiosulfate incubation of rat cortical slices and cell-free GSSG limitations: Concentration, duration and preparation matter; GPx activity is not evidence of selenium depletion. exposure: One- versus three-hour incubations; 10 micromolar sulfite redox observations evidence_span: {"source_cache": "artifacts/molybdenum-research/25777939.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1768480178724867d4c7a98f723cfd1a0010f7973eae4a4baea3d1261a06fdd2", "start_char": 0, "end_char": 2017, "text_sha256": "1768480178724867d4c7a98f723cfd1a0010f7973eae4a4baea3d1261a06fdd2"} [mo-p25777939] In vitro evidence that sulfite impairs glutamatergic neurotransmission and inhibits glutathione metabolism-related enzymes in rat cerebral cortex. (2015). https://pubmed.ncbi.nlm.nih.gov/25777939/ DOI: 10.1016/j.ijdevneu.2015.03.005
Complete structured claim and evidence
At 10 micromolar, sulfite lowered glutathione and increased lipid-peroxidation markers after one hour.
Sulfite / SO3(2-) → GSH source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/25777939.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1768480178724867d4c7a98f723cfd1a0010f7973eae4a4baea3d1261a06fdd2", "start_char": 0, "end_char": 2017, "text_sha256": "1768480178724867d4c7a98f723cfd1a0010f7973eae4a4baea3d1261a06fdd2"}
experimental_model
Sulfite/thiosulfate incubation of rat cortical slices and cell-free GSSG
exposure
One- versus three-hour incubations; 10 micromolar sulfite redox observations
limitations
Concentration, duration and preparation matter; GPx activity is not evidence of selenium depletion.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Rattus norvegicus; cell-free comparison
plain_language
The antioxidant pool changed in this tissue experiment.
primary_references
[mo-p25777939] In vitro evidence that sulfite impairs glutamatergic neurotransmission and inhibits glutathione metabolism-related enzymes in rat cerebral cortex. (2015). https://pubmed.ncbi.nlm.nih.gov/25777939/ DOI: 10.1016/j.ijdevneu.2015.03.005
tissue_or_cell_type
Cerebral cortex
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1405–1416
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Sulfite/thiosulfate incubation of rat cortical slices and cell-free GSSG · source_derived_draft · unverified_draft
### mo-sulfite-gsh At 10 micromolar, sulfite lowered glutathione and increased lipid-peroxidation markers after one hour. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The antioxidant pool changed in this tissue experiment. organism: Rattus norvegicus; cell-free comparison tissue_or_cell_type: Cerebral cortex experimental_model: Sulfite/thiosulfate incubation of rat cortical slices and cell-free GSSG limitations: Concentration, duration and preparation matter; GPx activity is not evidence of selenium depletion. exposure: One- versus three-hour incubations; 10 micromolar sulfite redox observations evidence_span: {"source_cache": "artifacts/molybdenum-research/25777939.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1768480178724867d4c7a98f723cfd1a0010f7973eae4a4baea3d1261a06fdd2", "start_char": 0, "end_char": 2017, "text_sha256": "1768480178724867d4c7a98f723cfd1a0010f7973eae4a4baea3d1261a06fdd2"} [mo-p25777939] In vitro evidence that sulfite impairs glutamatergic neurotransmission and inhibits glutathione metabolism-related enzymes in rat cerebral cortex. (2015). https://pubmed.ncbi.nlm.nih.gov/25777939/ DOI: 10.1016/j.ijdevneu.2015.03.005
Complete structured claim and evidence
GPx, GST and G6PD activities were unchanged after one hour but inhibited after three hours of sulfite exposure.
Sulfite / SO3(2-) → Rat cortical glutathione peroxidase enzymes source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/25777939.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1768480178724867d4c7a98f723cfd1a0010f7973eae4a4baea3d1261a06fdd2", "start_char": 0, "end_char": 2017, "text_sha256": "1768480178724867d4c7a98f723cfd1a0010f7973eae4a4baea3d1261a06fdd2"}
experimental_model
Sulfite/thiosulfate incubation of rat cortical slices and cell-free GSSG
exposure
One- versus three-hour incubations; 10 micromolar sulfite redox observations
limitations
Concentration, duration and preparation matter; GPx activity is not evidence of selenium depletion.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Rattus norvegicus; cell-free comparison
plain_language
A short experiment and a longer one can show different stages of the same response.
primary_references
[mo-p25777939] In vitro evidence that sulfite impairs glutamatergic neurotransmission and inhibits glutathione metabolism-related enzymes in rat cerebral cortex. (2015). https://pubmed.ncbi.nlm.nih.gov/25777939/ DOI: 10.1016/j.ijdevneu.2015.03.005
tissue_or_cell_type
Cerebral cortex
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1418–1429
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Sulfite/thiosulfate incubation of rat cortical slices and cell-free GSSG · source_derived_draft · unverified_draft
### mo-sulfite-gpx-time GPx, GST and G6PD activities were unchanged after one hour but inhibited after three hours of sulfite exposure. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: A short experiment and a longer one can show different stages of the same response. organism: Rattus norvegicus; cell-free comparison tissue_or_cell_type: Cerebral cortex experimental_model: Sulfite/thiosulfate incubation of rat cortical slices and cell-free GSSG limitations: Concentration, duration and preparation matter; GPx activity is not evidence of selenium depletion. exposure: One- versus three-hour incubations; 10 micromolar sulfite redox observations evidence_span: {"source_cache": "artifacts/molybdenum-research/25777939.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1768480178724867d4c7a98f723cfd1a0010f7973eae4a4baea3d1261a06fdd2", "start_char": 0, "end_char": 2017, "text_sha256": "1768480178724867d4c7a98f723cfd1a0010f7973eae4a4baea3d1261a06fdd2"} [mo-p25777939] In vitro evidence that sulfite impairs glutamatergic neurotransmission and inhibits glutathione metabolism-related enzymes in rat cerebral cortex. (2015). https://pubmed.ncbi.nlm.nih.gov/25777939/ DOI: 10.1016/j.ijdevneu.2015.03.005
Complete structured claim and evidence
At 500 micromolar, sulfite increased measured GSH in a cell-free GSSG solution, consistent with disulfide-bond chemistry.
Sulfite / SO3(2-) → GSSG source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/25777939.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1768480178724867d4c7a98f723cfd1a0010f7973eae4a4baea3d1261a06fdd2", "start_char": 0, "end_char": 2017, "text_sha256": "1768480178724867d4c7a98f723cfd1a0010f7973eae4a4baea3d1261a06fdd2"}
experimental_model
Sulfite/thiosulfate incubation of rat cortical slices and cell-free GSSG
exposure
One- versus three-hour incubations; 10 micromolar sulfite redox observations
limitations
Concentration, duration and preparation matter; GPx activity is not evidence of selenium depletion.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Rattus norvegicus; cell-free comparison
plain_language
A chemical increase in measured GSH outside cells is different from restoring a living antioxidant system.
primary_references
[mo-p25777939] In vitro evidence that sulfite impairs glutamatergic neurotransmission and inhibits glutathione metabolism-related enzymes in rat cerebral cortex. (2015). https://pubmed.ncbi.nlm.nih.gov/25777939/ DOI: 10.1016/j.ijdevneu.2015.03.005
tissue_or_cell_type
Cerebral cortex
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1431–1442
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Sulfite/thiosulfate incubation of rat cortical slices and cell-free GSSG · source_derived_draft · unverified_draft
### mo-sulfite-gssg-chemical At 500 micromolar, sulfite increased measured GSH in a cell-free GSSG solution, consistent with disulfide-bond chemistry. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: A chemical increase in measured GSH outside cells is different from restoring a living antioxidant system. organism: Rattus norvegicus; cell-free comparison tissue_or_cell_type: Cerebral cortex experimental_model: Sulfite/thiosulfate incubation of rat cortical slices and cell-free GSSG limitations: Concentration, duration and preparation matter; GPx activity is not evidence of selenium depletion. exposure: One- versus three-hour incubations; 10 micromolar sulfite redox observations evidence_span: {"source_cache": "artifacts/molybdenum-research/25777939.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1768480178724867d4c7a98f723cfd1a0010f7973eae4a4baea3d1261a06fdd2", "start_char": 0, "end_char": 2017, "text_sha256": "1768480178724867d4c7a98f723cfd1a0010f7973eae4a4baea3d1261a06fdd2"} [mo-p25777939] In vitro evidence that sulfite impairs glutamatergic neurotransmission and inhibits glutathione metabolism-related enzymes in rat cerebral cortex. (2015). https://pubmed.ncbi.nlm.nih.gov/25777939/ DOI: 10.1016/j.ijdevneu.2015.03.005
Complete structured claim and evidence
SO-deficient mouse fibroblasts had impaired ATP production and growth in galactose medium.
Mouse sulfite oxidase / Suox → Mitochondrial ATP production source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/33488670.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4cd0f95e723b56151456d582ec34bc7cd57c8e4a3d7e424b1d043a9cd5cfa962", "start_char": 0, "end_char": 1946, "text_sha256": "4cd0f95e723b56151456d582ec34bc7cd57c8e4a3d7e424b1d043a9cd5cfa962"}
experimental_model
SO-deficient mouse embryonic fibroblasts, sulfite titration and MoCD patient fibroblasts
exposure
Galactose culture and graded sulfite exposure
limitations
Network architecture is concentration dependent; fibroblast findings are not a direct human brain measurement.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Mus musculus and Homo sapiens in distinct experiments
plain_language
The defect became evident when cells relied more heavily on mitochondria.
primary_references
[mo-p33488670] Sulfite Alters the Mitochondrial Network in Molybdenum Cofactor Deficiency. (2020). https://pubmed.ncbi.nlm.nih.gov/33488670/ DOI: 10.3389/fgene.2020.594828
tissue_or_cell_type
Mitochondrial network and energy metabolism
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1444–1455
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · SO-deficient mouse embryonic fibroblasts, sulfite titration and MoCD patient fibroblasts · source_derived_draft · unverified_draft
### mo-suox-galactose SO-deficient mouse fibroblasts had impaired ATP production and growth in galactose medium. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The defect became evident when cells relied more heavily on mitochondria. organism: Mus musculus and Homo sapiens in distinct experiments tissue_or_cell_type: Mitochondrial network and energy metabolism experimental_model: SO-deficient mouse embryonic fibroblasts, sulfite titration and MoCD patient fibroblasts limitations: Network architecture is concentration dependent; fibroblast findings are not a direct human brain measurement. exposure: Galactose culture and graded sulfite exposure evidence_span: {"source_cache": "artifacts/molybdenum-research/33488670.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4cd0f95e723b56151456d582ec34bc7cd57c8e4a3d7e424b1d043a9cd5cfa962", "start_char": 0, "end_char": 1946, "text_sha256": "4cd0f95e723b56151456d582ec34bc7cd57c8e4a3d7e424b1d043a9cd5cfa962"} [mo-p33488670] Sulfite Alters the Mitochondrial Network in Molybdenum Cofactor Deficiency. (2020). https://pubmed.ncbi.nlm.nih.gov/33488670/ DOI: 10.3389/fgene.2020.594828
Complete structured claim and evidence
SO-deficient mouse fibroblasts formed a highly interconnected mitochondrial network; a similar pattern occurred in MoCD patient fibroblasts.
Mouse sulfite oxidase / Suox → Mitochondrial network interconnection source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/33488670.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4cd0f95e723b56151456d582ec34bc7cd57c8e4a3d7e424b1d043a9cd5cfa962", "start_char": 0, "end_char": 1946, "text_sha256": "4cd0f95e723b56151456d582ec34bc7cd57c8e4a3d7e424b1d043a9cd5cfa962"}
experimental_model
SO-deficient mouse embryonic fibroblasts, sulfite titration and MoCD patient fibroblasts
exposure
Galactose culture and graded sulfite exposure
limitations
Network architecture is concentration dependent; fibroblast findings are not a direct human brain measurement.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Mus musculus and Homo sapiens in distinct experiments
plain_language
The mitochondria changed how they connected to one another.
primary_references
[mo-p33488670] Sulfite Alters the Mitochondrial Network in Molybdenum Cofactor Deficiency. (2020). https://pubmed.ncbi.nlm.nih.gov/33488670/ DOI: 10.3389/fgene.2020.594828
tissue_or_cell_type
Mitochondrial network and energy metabolism
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1457–1468
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · SO-deficient mouse embryonic fibroblasts, sulfite titration and MoCD patient fibroblasts · source_derived_draft · unverified_draft
### mo-suox-network SO-deficient mouse fibroblasts formed a highly interconnected mitochondrial network; a similar pattern occurred in MoCD patient fibroblasts. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The mitochondria changed how they connected to one another. organism: Mus musculus and Homo sapiens in distinct experiments tissue_or_cell_type: Mitochondrial network and energy metabolism experimental_model: SO-deficient mouse embryonic fibroblasts, sulfite titration and MoCD patient fibroblasts limitations: Network architecture is concentration dependent; fibroblast findings are not a direct human brain measurement. exposure: Galactose culture and graded sulfite exposure evidence_span: {"source_cache": "artifacts/molybdenum-research/33488670.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4cd0f95e723b56151456d582ec34bc7cd57c8e4a3d7e424b1d043a9cd5cfa962", "start_char": 0, "end_char": 1946, "text_sha256": "4cd0f95e723b56151456d582ec34bc7cd57c8e4a3d7e424b1d043a9cd5cfa962"} [mo-p33488670] Sulfite Alters the Mitochondrial Network in Molybdenum Cofactor Deficiency. (2020). https://pubmed.ncbi.nlm.nih.gov/33488670/ DOI: 10.3389/fgene.2020.594828
Complete structured claim and evidence
Moderate sulfite elevation promoted interconnected networks, whereas high sulfite induced fragmentation.
Sulfite / SO3(2-) → Mitochondrial network fragmentation source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/33488670.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4cd0f95e723b56151456d582ec34bc7cd57c8e4a3d7e424b1d043a9cd5cfa962", "start_char": 0, "end_char": 1946, "text_sha256": "4cd0f95e723b56151456d582ec34bc7cd57c8e4a3d7e424b1d043a9cd5cfa962"}
experimental_model
SO-deficient mouse embryonic fibroblasts, sulfite titration and MoCD patient fibroblasts
exposure
Galactose culture and graded sulfite exposure
limitations
Network architecture is concentration dependent; fibroblast findings are not a direct human brain measurement.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Mus musculus and Homo sapiens in distinct experiments
plain_language
The same substance produced different mitochondrial patterns at different concentrations.
primary_references
[mo-p33488670] Sulfite Alters the Mitochondrial Network in Molybdenum Cofactor Deficiency. (2020). https://pubmed.ncbi.nlm.nih.gov/33488670/ DOI: 10.3389/fgene.2020.594828
tissue_or_cell_type
Mitochondrial network and energy metabolism
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1470–1481
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · SO-deficient mouse embryonic fibroblasts, sulfite titration and MoCD patient fibroblasts · source_derived_draft · unverified_draft
### mo-sulfite-network-dose Moderate sulfite elevation promoted interconnected networks, whereas high sulfite induced fragmentation. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The same substance produced different mitochondrial patterns at different concentrations. organism: Mus musculus and Homo sapiens in distinct experiments tissue_or_cell_type: Mitochondrial network and energy metabolism experimental_model: SO-deficient mouse embryonic fibroblasts, sulfite titration and MoCD patient fibroblasts limitations: Network architecture is concentration dependent; fibroblast findings are not a direct human brain measurement. exposure: Galactose culture and graded sulfite exposure evidence_span: {"source_cache": "artifacts/molybdenum-research/33488670.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4cd0f95e723b56151456d582ec34bc7cd57c8e4a3d7e424b1d043a9cd5cfa962", "start_char": 0, "end_char": 1946, "text_sha256": "4cd0f95e723b56151456d582ec34bc7cd57c8e4a3d7e424b1d043a9cd5cfa962"} [mo-p33488670] Sulfite Alters the Mitochondrial Network in Molybdenum Cofactor Deficiency. (2020). https://pubmed.ncbi.nlm.nih.gov/33488670/ DOI: 10.3389/fgene.2020.594828
Complete structured claim and evidence
Endogenous A165T MTARC1 showed substantial mislocalization outside the outer mitochondrial membrane in HepG2 cells.
Human MTARC1 p.Ala165Thr → Human MTARC1 outer mitochondrial membrane localization source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/38723751.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5c4b7e298ad8a9760c515d21299d8c831692c6c07361857e3f6ff6509e9438db", "start_char": 0, "end_char": 1564, "text_sha256": "5c4b7e298ad8a9760c515d21299d8c831692c6c07361857e3f6ff6509e9438db"}
experimental_model
Endogenous CRISPR knock-in variants in HepG2 cells
exposure
A165T versus WT and catalytically inactive C273A
limitations
Cellular protein effects; the protective mechanism in human liver disease was not proven.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
The altered protein was not positioned like the usual enzyme.
primary_references
[mo-p38723751] Biochemical and functional characterization of the p.A165T missense variant of mitochondrial amidoxime-reducing component 1. (2024). https://pubmed.ncbi.nlm.nih.gov/38723751/ DOI: 10.1016/j.jbc.2024.107353
tissue_or_cell_type
Hepatoma cells
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1483–1494
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Endogenous CRISPR knock-in variants in HepG2 cells · source_derived_draft · unverified_draft
### mo-marc-a165t-location Endogenous A165T MTARC1 showed substantial mislocalization outside the outer mitochondrial membrane in HepG2 cells. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The altered protein was not positioned like the usual enzyme. organism: Homo sapiens tissue_or_cell_type: Hepatoma cells experimental_model: Endogenous CRISPR knock-in variants in HepG2 cells limitations: Cellular protein effects; the protective mechanism in human liver disease was not proven. exposure: A165T versus WT and catalytically inactive C273A evidence_span: {"source_cache": "artifacts/molybdenum-research/38723751.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5c4b7e298ad8a9760c515d21299d8c831692c6c07361857e3f6ff6509e9438db", "start_char": 0, "end_char": 1564, "text_sha256": "5c4b7e298ad8a9760c515d21299d8c831692c6c07361857e3f6ff6509e9438db"} [mo-p38723751] Biochemical and functional characterization of the p.A165T missense variant of mitochondrial amidoxime-reducing component 1. (2024). https://pubmed.ncbi.nlm.nih.gov/38723751/ DOI: 10.1016/j.jbc.2024.107353
Complete structured claim and evidence
A165T MTARC1 showed increased ubiquitination and faster proteasomal degradation.
Human MTARC1 p.Ala165Thr → Proteasomal degradation of human MTARC1 source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/38723751.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5c4b7e298ad8a9760c515d21299d8c831692c6c07361857e3f6ff6509e9438db", "start_char": 0, "end_char": 1564, "text_sha256": "5c4b7e298ad8a9760c515d21299d8c831692c6c07361857e3f6ff6509e9438db"}
experimental_model
Endogenous CRISPR knock-in variants in HepG2 cells
exposure
A165T versus WT and catalytically inactive C273A
limitations
Cellular protein effects; the protective mechanism in human liver disease was not proven.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
The cell removed the variant protein faster.
primary_references
[mo-p38723751] Biochemical and functional characterization of the p.A165T missense variant of mitochondrial amidoxime-reducing component 1. (2024). https://pubmed.ncbi.nlm.nih.gov/38723751/ DOI: 10.1016/j.jbc.2024.107353
tissue_or_cell_type
Hepatoma cells
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1496–1507
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Endogenous CRISPR knock-in variants in HepG2 cells · source_derived_draft · unverified_draft
### mo-marc-a165t-turnover A165T MTARC1 showed increased ubiquitination and faster proteasomal degradation. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The cell removed the variant protein faster. organism: Homo sapiens tissue_or_cell_type: Hepatoma cells experimental_model: Endogenous CRISPR knock-in variants in HepG2 cells limitations: Cellular protein effects; the protective mechanism in human liver disease was not proven. exposure: A165T versus WT and catalytically inactive C273A evidence_span: {"source_cache": "artifacts/molybdenum-research/38723751.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5c4b7e298ad8a9760c515d21299d8c831692c6c07361857e3f6ff6509e9438db", "start_char": 0, "end_char": 1564, "text_sha256": "5c4b7e298ad8a9760c515d21299d8c831692c6c07361857e3f6ff6509e9438db"} [mo-p38723751] Biochemical and functional characterization of the p.A165T missense variant of mitochondrial amidoxime-reducing component 1. (2024). https://pubmed.ncbi.nlm.nih.gov/38723751/ DOI: 10.1016/j.jbc.2024.107353
Complete structured claim and evidence
Whole-body Marc1 knockout did not protect against hepatic triglyceride accumulation, inflammation or fibrosis in this mouse study.
Mouse mitochondrial amidoxime-reducing component 1 / Mtarc1 → Hepatic triglyceride accumulation source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/38437227.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "152bcc386bca67c8cd4891d284098784ebbdbf9c507f713f96b996bb3c75bd1b", "start_char": 0, "end_char": 1333, "text_sha256": "152bcc386bca67c8cd4891d284098784ebbdbf9c507f713f96b996bb3c75bd1b"}
experimental_model
Multi-ancestry exome association, human protein studies and whole-body mouse Marc1 knockout
exposure
MARC1 variants and mouse global knockout
limitations
Human association and mouse intervention are separate. The knockout null result differs from later published mouse knockout protection.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Human genetics in about 540000 individuals; Mus musculus knockout
plain_language
Removing MTARC1 did not help in this experiment.
primary_references
[mo-p38437227] Divergent role of Mitochondrial Amidoxime Reducing Component 1 (MARC1) in human and mouse. (2024). https://pubmed.ncbi.nlm.nih.gov/38437227/ DOI: 10.1371/journal.pgen.1011179
tissue_or_cell_type
Liver phenotypes
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1509–1520
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Multi-ancestry exome association, human protein studies and whole-body mouse Marc1 knockout · source_derived_draft · unverified_draft
### mo-marc-ko-null Whole-body Marc1 knockout did not protect against hepatic triglyceride accumulation, inflammation or fibrosis in this mouse study. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Removing MTARC1 did not help in this experiment. organism: Human genetics in about 540000 individuals; Mus musculus knockout tissue_or_cell_type: Liver phenotypes experimental_model: Multi-ancestry exome association, human protein studies and whole-body mouse Marc1 knockout limitations: Human association and mouse intervention are separate. The knockout null result differs from later published mouse knockout protection. exposure: MARC1 variants and mouse global knockout evidence_span: {"source_cache": "artifacts/molybdenum-research/38437227.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "152bcc386bca67c8cd4891d284098784ebbdbf9c507f713f96b996bb3c75bd1b", "start_char": 0, "end_char": 1333, "text_sha256": "152bcc386bca67c8cd4891d284098784ebbdbf9c507f713f96b996bb3c75bd1b"} [mo-p38437227] Divergent role of Mitochondrial Amidoxime Reducing Component 1 (MARC1) in human and mouse. (2024). https://pubmed.ncbi.nlm.nih.gov/38437227/ DOI: 10.1371/journal.pgen.1011179
Complete structured claim and evidence
The investigators found Marc2 to be the main Marc-family enzyme in mouse liver, with Marc1 contributing relatively little.
Mouse mitochondrial amidoxime-reducing component 2 / Mtarc2 → Mouse mitochondrial amidoxime-reducing component 1 / Mtarc1 source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/38437227.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "152bcc386bca67c8cd4891d284098784ebbdbf9c507f713f96b996bb3c75bd1b", "start_char": 0, "end_char": 1333, "text_sha256": "152bcc386bca67c8cd4891d284098784ebbdbf9c507f713f96b996bb3c75bd1b"}
experimental_model
Multi-ancestry exome association, human protein studies and whole-body mouse Marc1 knockout
exposure
MARC1 variants and mouse global knockout
limitations
Human association and mouse intervention are separate. The knockout null result differs from later published mouse knockout protection.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Human genetics in about 540000 individuals; Mus musculus knockout
plain_language
The balance between the two proteins differs across biological settings.
primary_references
[mo-p38437227] Divergent role of Mitochondrial Amidoxime Reducing Component 1 (MARC1) in human and mouse. (2024). https://pubmed.ncbi.nlm.nih.gov/38437227/ DOI: 10.1371/journal.pgen.1011179
tissue_or_cell_type
Liver phenotypes
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1522–1533
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Multi-ancestry exome association, human protein studies and whole-body mouse Marc1 knockout · source_derived_draft · unverified_draft
### mo-marc2-mouse-dominance The investigators found Marc2 to be the main Marc-family enzyme in mouse liver, with Marc1 contributing relatively little. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The balance between the two proteins differs across biological settings. organism: Human genetics in about 540000 individuals; Mus musculus knockout tissue_or_cell_type: Liver phenotypes experimental_model: Multi-ancestry exome association, human protein studies and whole-body mouse Marc1 knockout limitations: Human association and mouse intervention are separate. The knockout null result differs from later published mouse knockout protection. exposure: MARC1 variants and mouse global knockout evidence_span: {"source_cache": "artifacts/molybdenum-research/38437227.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "152bcc386bca67c8cd4891d284098784ebbdbf9c507f713f96b996bb3c75bd1b", "start_char": 0, "end_char": 1333, "text_sha256": "152bcc386bca67c8cd4891d284098784ebbdbf9c507f713f96b996bb3c75bd1b"} [mo-p38437227] Divergent role of Mitochondrial Amidoxime Reducing Component 1 (MARC1) in human and mouse. (2024). https://pubmed.ncbi.nlm.nih.gov/38437227/ DOI: 10.1371/journal.pgen.1011179
Complete structured claim and evidence
Global deletion and hepatocyte-specific knockdown of Mtarc1 reduced steatosis and fibrosis in multiple mouse models.
Mouse mitochondrial amidoxime-reducing component 1 / Mtarc1 → Hepatic triglyceride accumulation source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/39927988.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0ac1fb695999e1691580706469d581ce6bd90eeab03f7c26c1c79fbb4b4e169d", "start_char": 0, "end_char": 1938, "text_sha256": "0ac1fb695999e1691580706469d581ce6bd90eeab03f7c26c1c79fbb4b4e169d"}
experimental_model
Global deletion and hepatocyte-specific knockdown across mouse MASH/fibrosis models; cellular variants
exposure
Mtarc1 depletion under lipotoxic and diet/fibrosis challenges
limitations
Preclinical protein-targeting study. A165T retained mitochondrial localization in these experiments, unlike the endogenous HepG2 study; construct/model effects remain unresolved.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Mus musculus; human variant cell experiments
plain_language
Removing MTARC1 helped in these experiments.
primary_references
[mo-p39927988] Loss of mitochondrial amidoxime-reducing component 1 (mARC1) prevents disease progression by reducing fibrosis in multiple mouse models of chronic liver disease. (2025). https://pubmed.ncbi.nlm.nih.gov/39927988/ DOI: 10.1097/hc9.0000000000000637
tissue_or_cell_type
Liver and hepatocytes
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1535–1546
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Global deletion and hepatocyte-specific knockdown across mouse MASH/fibrosis models; cellular variants · source_derived_draft · unverified_draft
### mo-marc-ko-protection-2025 Global deletion and hepatocyte-specific knockdown of Mtarc1 reduced steatosis and fibrosis in multiple mouse models. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Removing MTARC1 helped in these experiments. organism: Mus musculus; human variant cell experiments tissue_or_cell_type: Liver and hepatocytes experimental_model: Global deletion and hepatocyte-specific knockdown across mouse MASH/fibrosis models; cellular variants limitations: Preclinical protein-targeting study. A165T retained mitochondrial localization in these experiments, unlike the endogenous HepG2 study; construct/model effects remain unresolved. exposure: Mtarc1 depletion under lipotoxic and diet/fibrosis challenges evidence_span: {"source_cache": "artifacts/molybdenum-research/39927988.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0ac1fb695999e1691580706469d581ce6bd90eeab03f7c26c1c79fbb4b4e169d", "start_char": 0, "end_char": 1938, "text_sha256": "0ac1fb695999e1691580706469d581ce6bd90eeab03f7c26c1c79fbb4b4e169d"} [mo-p39927988] Loss of mitochondrial amidoxime-reducing component 1 (mARC1) prevents disease progression by reducing fibrosis in multiple mouse models of chronic liver disease. (2025). https://pubmed.ncbi.nlm.nih.gov/39927988/ DOI: 10.1097/hc9.0000000000000637
Complete structured claim and evidence
Global and liver-specific Mtarc1 knockout protected against diet-induced triglyceride accumulation, inflammation and fibrosis.
Mouse mitochondrial amidoxime-reducing component 1 / Mtarc1 → Hepatic triglyceride accumulation source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/41641916.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "52b4d4d00867faaa1bb51ff6055f887a72c4c0d266bf7a1665b3780ce03aee64", "start_char": 0, "end_char": 1681, "text_sha256": "52b4d4d00867faaa1bb51ff6055f887a72c4c0d266bf7a1665b3780ce03aee64"}
experimental_model
Global/liver Mtarc1 knockout with Pnpla2, Lipa, Pemt and Cept1 interventions
exposure
Diet-induced liver disease with gene knockouts/knockdowns and multi-omics
limitations
Preclinical mechanism; no evidence that dietary molybdenum restriction selectively reproduces MTARC1 targeting.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Mus musculus; supporting cell studies
plain_language
This study also found protection after targeted MTARC1 loss.
primary_references
[mo-p41641916] MTARC1 Inactivation Remodels Lipid Droplets to Protect Against Metabolic Fatty Liver Disease. (2026). https://pubmed.ncbi.nlm.nih.gov/41641916/ DOI: 10.1111/liv.70539
tissue_or_cell_type
Hepatic lipid droplets
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1548–1559
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Global/liver Mtarc1 knockout with Pnpla2, Lipa, Pemt and Cept1 interventions · source_derived_draft · unverified_draft
### mo-marc-ko-protection-2026 Global and liver-specific Mtarc1 knockout protected against diet-induced triglyceride accumulation, inflammation and fibrosis. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: This study also found protection after targeted MTARC1 loss. organism: Mus musculus; supporting cell studies tissue_or_cell_type: Hepatic lipid droplets experimental_model: Global/liver Mtarc1 knockout with Pnpla2, Lipa, Pemt and Cept1 interventions limitations: Preclinical mechanism; no evidence that dietary molybdenum restriction selectively reproduces MTARC1 targeting. exposure: Diet-induced liver disease with gene knockouts/knockdowns and multi-omics evidence_span: {"source_cache": "artifacts/molybdenum-research/41641916.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "52b4d4d00867faaa1bb51ff6055f887a72c4c0d266bf7a1665b3780ce03aee64", "start_char": 0, "end_char": 1681, "text_sha256": "52b4d4d00867faaa1bb51ff6055f887a72c4c0d266bf7a1665b3780ce03aee64"} [mo-p41641916] MTARC1 Inactivation Remodels Lipid Droplets to Protect Against Metabolic Fatty Liver Disease. (2026). https://pubmed.ncbi.nlm.nih.gov/41641916/ DOI: 10.1111/liv.70539
Complete structured claim and evidence
Mtarc1 loss post-transcriptionally increased CEPT1 and PEMT, altering lipid-droplet phospholipids; knocking down these enzymes reversed protection.
Mouse mitochondrial amidoxime-reducing component 1 / Mtarc1 → Mouse choline/ethanolamine phosphotransferase 1 / Cept1 source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/41641916.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "52b4d4d00867faaa1bb51ff6055f887a72c4c0d266bf7a1665b3780ce03aee64", "start_char": 0, "end_char": 1681, "text_sha256": "52b4d4d00867faaa1bb51ff6055f887a72c4c0d266bf7a1665b3780ce03aee64"}
experimental_model
Global/liver Mtarc1 knockout with Pnpla2, Lipa, Pemt and Cept1 interventions
exposure
Diet-induced liver disease with gene knockouts/knockdowns and multi-omics
limitations
Preclinical mechanism; no evidence that dietary molybdenum restriction selectively reproduces MTARC1 targeting.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Mus musculus; supporting cell studies
plain_language
Changing the droplet surface helped connect the enzyme loss to fat handling.
primary_references
[mo-p41641916] MTARC1 Inactivation Remodels Lipid Droplets to Protect Against Metabolic Fatty Liver Disease. (2026). https://pubmed.ncbi.nlm.nih.gov/41641916/ DOI: 10.1111/liv.70539
tissue_or_cell_type
Hepatic lipid droplets
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1561–1572
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Global/liver Mtarc1 knockout with Pnpla2, Lipa, Pemt and Cept1 interventions · source_derived_draft · unverified_draft
### mo-marc-lipid-enzymes Mtarc1 loss post-transcriptionally increased CEPT1 and PEMT, altering lipid-droplet phospholipids; knocking down these enzymes reversed protection. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Changing the droplet surface helped connect the enzyme loss to fat handling. organism: Mus musculus; supporting cell studies tissue_or_cell_type: Hepatic lipid droplets experimental_model: Global/liver Mtarc1 knockout with Pnpla2, Lipa, Pemt and Cept1 interventions limitations: Preclinical mechanism; no evidence that dietary molybdenum restriction selectively reproduces MTARC1 targeting. exposure: Diet-induced liver disease with gene knockouts/knockdowns and multi-omics evidence_span: {"source_cache": "artifacts/molybdenum-research/41641916.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "52b4d4d00867faaa1bb51ff6055f887a72c4c0d266bf7a1665b3780ce03aee64", "start_char": 0, "end_char": 1681, "text_sha256": "52b4d4d00867faaa1bb51ff6055f887a72c4c0d266bf7a1665b3780ce03aee64"} [mo-p41641916] MTARC1 Inactivation Remodels Lipid Droplets to Protect Against Metabolic Fatty Liver Disease. (2026). https://pubmed.ncbi.nlm.nih.gov/41641916/ DOI: 10.1111/liv.70539
Complete structured claim and evidence
The protection required triglyceride breakdown through lipolysis and lipophagy, tested with Pnpla2 and Lipa inhibition.
Mouse mitochondrial amidoxime-reducing component 1 / Mtarc1 → Hepatic lipid-droplet degradation source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/41641916.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "52b4d4d00867faaa1bb51ff6055f887a72c4c0d266bf7a1665b3780ce03aee64", "start_char": 0, "end_char": 1681, "text_sha256": "52b4d4d00867faaa1bb51ff6055f887a72c4c0d266bf7a1665b3780ce03aee64"}
experimental_model
Global/liver Mtarc1 knockout with Pnpla2, Lipa, Pemt and Cept1 interventions
exposure
Diet-induced liver disease with gene knockouts/knockdowns and multi-omics
limitations
Preclinical mechanism; no evidence that dietary molybdenum restriction selectively reproduces MTARC1 targeting.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Mus musculus; supporting cell studies
plain_language
Fat had to be broken down for the protective effect to occur.
primary_references
[mo-p41641916] MTARC1 Inactivation Remodels Lipid Droplets to Protect Against Metabolic Fatty Liver Disease. (2026). https://pubmed.ncbi.nlm.nih.gov/41641916/ DOI: 10.1111/liv.70539
tissue_or_cell_type
Hepatic lipid droplets
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1574–1585
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Global/liver Mtarc1 knockout with Pnpla2, Lipa, Pemt and Cept1 interventions · source_derived_draft · unverified_draft
### mo-marc-lipolysis The protection required triglyceride breakdown through lipolysis and lipophagy, tested with Pnpla2 and Lipa inhibition. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Fat had to be broken down for the protective effect to occur. organism: Mus musculus; supporting cell studies tissue_or_cell_type: Hepatic lipid droplets experimental_model: Global/liver Mtarc1 knockout with Pnpla2, Lipa, Pemt and Cept1 interventions limitations: Preclinical mechanism; no evidence that dietary molybdenum restriction selectively reproduces MTARC1 targeting. exposure: Diet-induced liver disease with gene knockouts/knockdowns and multi-omics evidence_span: {"source_cache": "artifacts/molybdenum-research/41641916.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "52b4d4d00867faaa1bb51ff6055f887a72c4c0d266bf7a1665b3780ce03aee64", "start_char": 0, "end_char": 1681, "text_sha256": "52b4d4d00867faaa1bb51ff6055f887a72c4c0d266bf7a1665b3780ce03aee64"} [mo-p41641916] MTARC1 Inactivation Remodels Lipid Droplets to Protect Against Metabolic Fatty Liver Disease. (2026). https://pubmed.ncbi.nlm.nih.gov/41641916/ DOI: 10.1111/liv.70539
Complete structured claim and evidence
A168T mice had lower MTARC1 protein despite unchanged mRNA, but neither sex showed significant protection from steatosis, inflammation or fibrosis.
Mouse Mtarc1 p.Ala168Thr → Hepatic triglyceride accumulation source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/molybdenum-research/41428769.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5ac3e4efcae2e5b23a255c61586bbff33d3114fe2c8e28befe2d9ad501f774bd", "start_char": 0, "end_char": 1816, "text_sha256": "5ac3e4efcae2e5b23a255c61586bbff33d3114fe2c8e28befe2d9ad501f774bd"}
experimental_model
Male/female mouse A168T knock-in in multiple MASH/fibrosis models
exposure
Mouse ortholog of human A165T; no global knockout
limitations
Partial variant effects are not identical to deleting the gene. No human molybdenum intervention.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Mus musculus
plain_language
Lower protein from this variant was not enough to reproduce knockout protection.
primary_references
[mo-p41428769] A mitochondrial amidoxime-reducing component 1 (mARC1) A168T amino acid substitution does not confer protection from MASH and fibrosis in multiple mouse models of chronic liver disease. (2026). https://pubmed.ncbi.nlm.nih.gov/41428769/ DOI: 10.1042/bcj20253411
tissue_or_cell_type
Liver disease and protein expression
trigger_kind
machinery_impairment Imported condition classification; unverified.
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1587–1598
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Male/female mouse A168T knock-in in multiple MASH/fibrosis models · source_derived_draft · unverified_draft
### mo-marc-a168t-null A168T mice had lower MTARC1 protein despite unchanged mRNA, but neither sex showed significant protection from steatosis, inflammation or fibrosis. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Lower protein from this variant was not enough to reproduce knockout protection. organism: Mus musculus tissue_or_cell_type: Liver disease and protein expression experimental_model: Male/female mouse A168T knock-in in multiple MASH/fibrosis models limitations: Partial variant effects are not identical to deleting the gene. No human molybdenum intervention. exposure: Mouse ortholog of human A165T; no global knockout evidence_span: {"source_cache": "artifacts/molybdenum-research/41428769.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5ac3e4efcae2e5b23a255c61586bbff33d3114fe2c8e28befe2d9ad501f774bd", "start_char": 0, "end_char": 1816, "text_sha256": "5ac3e4efcae2e5b23a255c61586bbff33d3114fe2c8e28befe2d9ad501f774bd"} [mo-p41428769] A mitochondrial amidoxime-reducing component 1 (mARC1) A168T amino acid substitution does not confer protection from MASH and fibrosis in multiple mouse models of chronic liver disease. (2026). https://pubmed.ncbi.nlm.nih.gov/41428769/ DOI: 10.1042/bcj20253411
Complete structured claim and evidence
Tetrathiomolybdate formed a stable sulfur-bridged copper-molybdenum cluster with yeast Atx1.
Tetrathiomolybdate / MoS4(2-) → Saccharomyces cerevisiae copper chaperone / Atx1 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/19965379.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "166eb55335870bc9843fdb0c61becaa318603b25c601bbfa8f69a469dab89e57", "start_char": 0, "end_char": 950, "text_sha256": "166eb55335870bc9843fdb0c61becaa318603b25c601bbfa8f69a469dab89e57"}
experimental_model
Yeast Atx1 crystallography, spectroscopy and copper-transfer experiments
exposure
Tetrathiomolybdate exposure
limitations
Drug and yeast-protein chemistry; not evidence that normal human dietary molybdate strips copper from proteins.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Saccharomyces cerevisiae proteins; comparison with animal drug complexes
plain_language
A sulfur-rich molybdenum drug can trap copper in a protein complex.
primary_references
[mo-p19965379] Tetrathiomolybdate inhibits copper trafficking proteins through metal cluster formation. (2010). https://pubmed.ncbi.nlm.nih.gov/19965379/ DOI: 10.1126/science.1179907
tissue_or_cell_type
Purified copper chaperones
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1600–1611
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Yeast Atx1 crystallography, spectroscopy and copper-transfer experiments · source_derived_draft · unverified_draft
### mo-ttm-copper-cluster Tetrathiomolybdate formed a stable sulfur-bridged copper-molybdenum cluster with yeast Atx1. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: A sulfur-rich molybdenum drug can trap copper in a protein complex. organism: Saccharomyces cerevisiae proteins; comparison with animal drug complexes tissue_or_cell_type: Purified copper chaperones experimental_model: Yeast Atx1 crystallography, spectroscopy and copper-transfer experiments limitations: Drug and yeast-protein chemistry; not evidence that normal human dietary molybdate strips copper from proteins. exposure: Tetrathiomolybdate exposure evidence_span: {"source_cache": "artifacts/molybdenum-research/19965379.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "166eb55335870bc9843fdb0c61becaa318603b25c601bbfa8f69a469dab89e57", "start_char": 0, "end_char": 950, "text_sha256": "166eb55335870bc9843fdb0c61becaa318603b25c601bbfa8f69a469dab89e57"} [mo-p19965379] Tetrathiomolybdate inhibits copper trafficking proteins through metal cluster formation. (2010). https://pubmed.ncbi.nlm.nih.gov/19965379/ DOI: 10.1126/science.1179907
Complete structured claim and evidence
The drug-Atx1 complex inhibited copper transfer between copper-trafficking proteins in the experimental system.
Tetrathiomolybdate-copper-yeast Atx1 cluster → Saccharomyces cerevisiae copper-transporting ATPase / Ccc2 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/19965379.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "166eb55335870bc9843fdb0c61becaa318603b25c601bbfa8f69a469dab89e57", "start_char": 0, "end_char": 950, "text_sha256": "166eb55335870bc9843fdb0c61becaa318603b25c601bbfa8f69a469dab89e57"}
experimental_model
Yeast Atx1 crystallography, spectroscopy and copper-transfer experiments
exposure
Tetrathiomolybdate exposure
limitations
Drug and yeast-protein chemistry; not evidence that normal human dietary molybdate strips copper from proteins.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Saccharomyces cerevisiae proteins; comparison with animal drug complexes
plain_language
Trapping the copper interrupted its handoff to another protein.
primary_references
[mo-p19965379] Tetrathiomolybdate inhibits copper trafficking proteins through metal cluster formation. (2010). https://pubmed.ncbi.nlm.nih.gov/19965379/ DOI: 10.1126/science.1179907
tissue_or_cell_type
Purified copper chaperones
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1613–1624
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Yeast Atx1 crystallography, spectroscopy and copper-transfer experiments · source_derived_draft · unverified_draft
### mo-ttm-copper-transfer The drug-Atx1 complex inhibited copper transfer between copper-trafficking proteins in the experimental system. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Trapping the copper interrupted its handoff to another protein. organism: Saccharomyces cerevisiae proteins; comparison with animal drug complexes tissue_or_cell_type: Purified copper chaperones experimental_model: Yeast Atx1 crystallography, spectroscopy and copper-transfer experiments limitations: Drug and yeast-protein chemistry; not evidence that normal human dietary molybdate strips copper from proteins. exposure: Tetrathiomolybdate exposure evidence_span: {"source_cache": "artifacts/molybdenum-research/19965379.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "166eb55335870bc9843fdb0c61becaa318603b25c601bbfa8f69a469dab89e57", "start_char": 0, "end_char": 950, "text_sha256": "166eb55335870bc9843fdb0c61becaa318603b25c601bbfa8f69a469dab89e57"} [mo-p19965379] Tetrathiomolybdate inhibits copper trafficking proteins through metal cluster formation. (2010). https://pubmed.ncbi.nlm.nih.gov/19965379/ DOI: 10.1126/science.1179907
Complete structured claim and evidence
Radiotracer experiments directly detected tri- and tetrathiomolybdate formation in the sheep rumen after molybdate administration.
Molybdate / MoO4(2-) → Tetrathiomolybdate / MoS4(2-) source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/3620434.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ef45902ca0d465ae0c4c59c2f669a74137ba1b0f64d7aff5502c2cf57154ef25", "start_char": 0, "end_char": 1324, "text_sha256": "ef45902ca0d465ae0c4c59c2f669a74137ba1b0f64d7aff5502c2cf57154ef25"}
experimental_model
Radiolabeled molybdate/thiomolybdate administered into sheep rumen
exposure
Grass diet plus intraruminal 99Mo compounds
limitations
Ruminant sulfur chemistry cannot be assumed to occur to the same extent in the human gut.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Ovis aries
plain_language
Rumen microbes create copper-interacting forms under these animal conditions.
primary_references
[mo-p3620434] Identification of thiomolybdates in digesta and plasma from sheep after administration of 99Mo-labelled compounds into the rumen. (1987). https://pubmed.ncbi.nlm.nih.gov/3620434/ DOI: 10.1079/bjn19870076
tissue_or_cell_type
Rumen, intestinal digesta and plasma
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1626–1637
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Radiolabeled molybdate/thiomolybdate administered into sheep rumen · source_derived_draft · unverified_draft
### mo-rumen-thiomolybdates Radiotracer experiments directly detected tri- and tetrathiomolybdate formation in the sheep rumen after molybdate administration. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Rumen microbes create copper-interacting forms under these animal conditions. organism: Ovis aries tissue_or_cell_type: Rumen, intestinal digesta and plasma experimental_model: Radiolabeled molybdate/thiomolybdate administered into sheep rumen limitations: Ruminant sulfur chemistry cannot be assumed to occur to the same extent in the human gut. exposure: Grass diet plus intraruminal 99Mo compounds evidence_span: {"source_cache": "artifacts/molybdenum-research/3620434.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ef45902ca0d465ae0c4c59c2f669a74137ba1b0f64d7aff5502c2cf57154ef25", "start_char": 0, "end_char": 1324, "text_sha256": "ef45902ca0d465ae0c4c59c2f669a74137ba1b0f64d7aff5502c2cf57154ef25"} [mo-p3620434] Identification of thiomolybdates in digesta and plasma from sheep after administration of 99Mo-labelled compounds into the rumen. (1987). https://pubmed.ncbi.nlm.nih.gov/3620434/ DOI: 10.1079/bjn19870076
Complete structured claim and evidence
Twenty of 28 participants met the copper endpoint; mean corrected non-ceruloplasmin copper fell 72% at 24 weeks.
Bis-choline tetrathiomolybdate → Corrected non-ceruloplasmin-bound plasma copper source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/28988934.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6ca2c31c7a405be35fb18be79af77bbac1efc1dceb26a625f5a5cd35121cba7c", "start_char": 0, "end_char": 3591, "text_sha256": "6ca2c31c7a405be35fb18be79af77bbac1efc1dceb26a625f5a5cd35121cba7c"}
experimental_model
Open-label phase 2 trial in 28 adults with Wilson disease
exposure
24 weeks of response-adjusted bis-choline tetrathiomolybdate
limitations
No blinded comparator. Pharmacological copper-binding drug, not nutritional molybdenum; endpoint corrects for drug-bound copper.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
The drug changed a copper measure in patients with a copper-accumulation disorder.
primary_references
[mo-p28988934] Bis-choline tetrathiomolybdate in patients with Wilson's disease: an open-label, multicentre, phase 2 study. (2017). https://pubmed.ncbi.nlm.nih.gov/28988934/ DOI: 10.1016/s2468-1253(17)30293-5
tissue_or_cell_type
Plasma copper and clinical safety
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1639–1650
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Open-label phase 2 trial in 28 adults with Wilson disease · source_derived_draft · unverified_draft
### mo-ttm-human-copper Twenty of 28 participants met the copper endpoint; mean corrected non-ceruloplasmin copper fell 72% at 24 weeks. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The drug changed a copper measure in patients with a copper-accumulation disorder. organism: Homo sapiens tissue_or_cell_type: Plasma copper and clinical safety experimental_model: Open-label phase 2 trial in 28 adults with Wilson disease limitations: No blinded comparator. Pharmacological copper-binding drug, not nutritional molybdenum; endpoint corrects for drug-bound copper. exposure: 24 weeks of response-adjusted bis-choline tetrathiomolybdate evidence_span: {"source_cache": "artifacts/molybdenum-research/28988934.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6ca2c31c7a405be35fb18be79af77bbac1efc1dceb26a625f5a5cd35121cba7c", "start_char": 0, "end_char": 3591, "text_sha256": "6ca2c31c7a405be35fb18be79af77bbac1efc1dceb26a625f5a5cd35121cba7c"} [mo-p28988934] Bis-choline tetrathiomolybdate in patients with Wilson's disease: an open-label, multicentre, phase 2 study. (2017). https://pubmed.ncbi.nlm.nih.gov/28988934/ DOI: 10.1016/s2468-1253(17)30293-5
Complete structured claim and evidence
Reversible asymptomatic liver-enzyme increases occurred in 11/28 patients receiving at least 30 mg/day; seven patients had serious adverse events of mixed attribution.
Bis-choline tetrathiomolybdate → Serum liver enzyme elevation source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/molybdenum-research/28988934.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6ca2c31c7a405be35fb18be79af77bbac1efc1dceb26a625f5a5cd35121cba7c", "start_char": 0, "end_char": 3591, "text_sha256": "6ca2c31c7a405be35fb18be79af77bbac1efc1dceb26a625f5a5cd35121cba7c"}
experimental_model
Open-label phase 2 trial in 28 adults with Wilson disease
exposure
24 weeks of response-adjusted bis-choline tetrathiomolybdate
limitations
No blinded comparator. Pharmacological copper-binding drug, not nutritional molybdenum; endpoint corrects for drug-bound copper.
nutrient_topic
Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
organism
Homo sapiens
plain_language
The drug results include adverse effects as well as copper reduction.
primary_references
[mo-p28988934] Bis-choline tetrathiomolybdate in patients with Wilson's disease: an open-label, multicentre, phase 2 study. (2017). https://pubmed.ncbi.nlm.nih.gov/28988934/ DOI: 10.1016/s2468-1253(17)30293-5
tissue_or_cell_type
Plasma copper and clinical safety
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1652–1663
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Open-label phase 2 trial in 28 adults with Wilson disease · source_derived_draft · unverified_draft
### mo-ttm-human-safety Reversible asymptomatic liver-enzyme increases occurred in 11/28 patients receiving at least 30 mg/day; seven patients had serious adverse events of mixed attribution. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The drug results include adverse effects as well as copper reduction. organism: Homo sapiens tissue_or_cell_type: Plasma copper and clinical safety experimental_model: Open-label phase 2 trial in 28 adults with Wilson disease limitations: No blinded comparator. Pharmacological copper-binding drug, not nutritional molybdenum; endpoint corrects for drug-bound copper. exposure: 24 weeks of response-adjusted bis-choline tetrathiomolybdate evidence_span: {"source_cache": "artifacts/molybdenum-research/28988934.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6ca2c31c7a405be35fb18be79af77bbac1efc1dceb26a625f5a5cd35121cba7c", "start_char": 0, "end_char": 3591, "text_sha256": "6ca2c31c7a405be35fb18be79af77bbac1efc1dceb26a625f5a5cd35121cba7c"} [mo-p28988934] Bis-choline tetrathiomolybdate in patients with Wilson's disease: an open-label, multicentre, phase 2 study. (2017). https://pubmed.ncbi.nlm.nih.gov/28988934/ DOI: 10.1016/s2468-1253(17)30293-5
Complete structured claim and evidence
In the recombinant hybrid NFS1–ISD11–ACP structure, the phosphopantetheine-linked acyl group of E. coli ACP occupies the hydrophobic core of human ISD11.
Escherichia coli acylated phosphopantetheinyl-AcpP → Human ISD11 / LYRM4 source_derived_draftungraded
Experimental context and source evidence
cross_nutrient
true
evidence_location
Abstract; primary Results: Identification of the ACP–Lipid–ISD11 Motif
experimental_model
Hybrid recombinant human NFS1–ISD11 plus native E. coli ACP; X-ray/EM structure
exposure
Coexpression and structural analysis; no nutrient restriction.
limitations
This is not an all-human ACP structure. The bound PLP and acyl-ACP show cofactor coexistence; dietary B6/B5 dependency or repletion was not tested. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation.
nutrient_topic
Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. · Pantothenate (vitamin B5)
organism
Homo sapiens proteins; Escherichia coli ACP
plain_language
The CoA-derived carrier arm holds a fatty-acid chain that helps form the iron–sulfur complex interface.
primary_references
[b5-met-cory2017] Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions. (2017). https://pubmed.ncbi.nlm.nih.gov/28634302/ DOI: 10.1073/pnas.1702849114
tissue_or_cell_type
Purified recombinant Fe–S assembly subcomplex
Pantothenic acid (vitamin B5): coenzyme A, deficiency and nutrient interactions (2026-09-17) · lines 935–947
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Hybrid recombinant human NFS1–ISD11 plus native E. coli ACP; X-ray/EM structure · source_derived_draft · unverified_draft
### b5-met-acyl-acp-isd11-interface In the recombinant hybrid NFS1–ISD11–ACP structure, the phosphopantetheine-linked acyl group of E. coli ACP occupies the hydrophobic core of human ISD11. Condition category: normal nutrient_topic: Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. plain_language: The CoA-derived carrier arm holds a fatty-acid chain that helps form the iron–sulfur complex interface. organism: Homo sapiens proteins; Escherichia coli ACP tissue_or_cell_type: Purified recombinant Fe–S assembly subcomplex experimental_model: Hybrid recombinant human NFS1–ISD11 plus native E. coli ACP; X-ray/EM structure limitations: This is not an all-human ACP structure. The bound PLP and acyl-ACP show cofactor coexistence; dietary B6/B5 dependency or repletion was not tested. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation. exposure: Coexpression and structural analysis; no nutrient restriction. cross_nutrient: true evidence_location: Abstract; primary Results: Identification of the ACP–Lipid–ISD11 Motif [b5-met-cory2017] Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions. (2017). https://pubmed.ncbi.nlm.nih.gov/28634302/ DOI: 10.1073/pnas.1702849114
Complete structured claim and evidence
Ndufab1 siRNA in mouse C2C12 myoblasts reduced mitochondrial Nfs1, Isd11 and Iscu2 protein abundance.
Mouse mitochondrial acyl carrier protein / Ndufab1 → Mouse cysteine desulfurase / Nfs1 source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
cross_nutrient
true
evidence_location
Full text line 117; Fig. 3C
experimental_model
Pooled Ndufab1 siRNA versus scrambled control
exposure
Ndufab1-targeting siRNA; immunoblot of isolated mitochondria.
limitations
The mammalian intact Nfs1–Isd11 complex could not be resolved by the authors with BN-PAGE; the direct mammalian result is subunit abundance. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation.
nutrient_topic
Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. · Pantothenate (vitamin B5)
organism
Mus musculus
plain_language
The iron–sulfur machinery also became less stable after carrier depletion in mouse muscle cells.
primary_references
[b5-met-acp2016] The mitochondrial acyl carrier protein (ACP) coordinates mitochondrial fatty acid synthesis with iron sulfur cluster biogenesis. (2016). https://pubmed.ncbi.nlm.nih.gov/27540631/ DOI: 10.7554/elife.17828
tissue_or_cell_type
C2C12 myoblast mitochondria
trigger_kind
machinery_impairment Imported condition classification; unverified.
Pantothenic acid (vitamin B5): coenzyme A, deficiency and nutrient interactions (2026-09-17) · lines 921–933
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Pooled Ndufab1 siRNA versus scrambled control · source_derived_draft · unverified_draft
### b5-met-mouse-acp-isu-stability Ndufab1 siRNA in mouse C2C12 myoblasts reduced mitochondrial Nfs1, Isd11 and Iscu2 protein abundance. Condition category: machinery_impairment nutrient_topic: Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. plain_language: The iron–sulfur machinery also became less stable after carrier depletion in mouse muscle cells. organism: Mus musculus tissue_or_cell_type: C2C12 myoblast mitochondria experimental_model: Pooled Ndufab1 siRNA versus scrambled control limitations: The mammalian intact Nfs1–Isd11 complex could not be resolved by the authors with BN-PAGE; the direct mammalian result is subunit abundance. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation. exposure: Ndufab1-targeting siRNA; immunoblot of isolated mitochondria. cross_nutrient: true evidence_location: Full text line 117; Fig. 3C [b5-met-acp2016] The mitochondrial acyl carrier protein (ACP) coordinates mitochondrial fatty acid synthesis with iron sulfur cluster biogenesis. (2016). https://pubmed.ncbi.nlm.nih.gov/27540631/ DOI: 10.7554/elife.17828
Complete structured claim and evidence
PLP-dependent human CBS condenses serine with homocysteine to produce cystathionine.
Human cystathionine beta-synthase / CBS → Cystathionine source_derived_draftungraded
Experimental context and source evidence
cross_nutrient
Methionine-derived sulfur enters cysteine synthesis.
experimental_model
Recombinant truncated human CBS crystallography
limitations
Enzyme chemistry alone does not predict whole-body homocysteine during mild deficiency.
nutrient_topic
Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B6
organism
Homo sapiens
plain_language
This B6-dependent step channels homocysteine into transsulfuration.
primary_references
[b6-cbs-2001] Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein. (2001). https://pmc.ncbi.nlm.nih.gov/articles/PMC149156/ DOI: 10.1093/emboj/20.15.3910
tissue_or_cell_type
Purified recombinant protein; no intact tissue
Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 517–527
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant truncated human CBS crystallography · source_derived_draft · unverified_draft
### b6-met-cbs-condensation PLP-dependent human CBS condenses serine with homocysteine to produce cystathionine. Condition category: normal nutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. plain_language: This B6-dependent step channels homocysteine into transsulfuration. organism: Homo sapiens tissue_or_cell_type: Purified recombinant protein; no intact tissue experimental_model: Recombinant truncated human CBS crystallography limitations: Enzyme chemistry alone does not predict whole-body homocysteine during mild deficiency. cross_nutrient: Methionine-derived sulfur enters cysteine synthesis. [b6-cbs-2001] Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein. (2001). https://pmc.ncbi.nlm.nih.gov/articles/PMC149156/ DOI: 10.1093/emboj/20.15.3910
Complete structured claim and evidence
The human CBS catalytic core binds PLP through its active-site lysine; this site is separate from the heme-binding region.
PLP → Human cystathionine beta-synthase / CBS source_derived_draftungraded
Experimental context and source evidence
cross_nutrient
Vitamin B6 and sulfur amino-acid metabolism.
experimental_model
Recombinant truncated human CBS crystallography
limitations
The crystallized human construct lacks the C-terminal regulatory region.
nutrient_topic
Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B6
organism
Homo sapiens
plain_language
CBS uses active vitamin B6 in its catalytic site.
primary_references
[b6-cbs-2001] Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein. (2001). https://pmc.ncbi.nlm.nih.gov/articles/PMC149156/ DOI: 10.1093/emboj/20.15.3910
tissue_or_cell_type
Purified recombinant protein; no intact tissue
Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 505–515
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant truncated human CBS crystallography · source_derived_draft · unverified_draft
### b6-met-cbs-plp The human CBS catalytic core binds PLP through its active-site lysine; this site is separate from the heme-binding region. Condition category: normal nutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. plain_language: CBS uses active vitamin B6 in its catalytic site. organism: Homo sapiens tissue_or_cell_type: Purified recombinant protein; no intact tissue experimental_model: Recombinant truncated human CBS crystallography limitations: The crystallized human construct lacks the C-terminal regulatory region. cross_nutrient: Vitamin B6 and sulfur amino-acid metabolism. [b6-cbs-2001] Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein. (2001). https://pmc.ncbi.nlm.nih.gov/articles/PMC149156/ DOI: 10.1093/emboj/20.15.3910
Complete structured claim and evidence
Human CTH cleaves cystathionine to cysteine, 2-oxobutanoate and ammonia in a PLP-dependent reaction.
Human cystathionine gamma-lyase / CTH → Cystathionine source_derived_draftungraded
Experimental context and source evidence
cross_nutrient
B6-dependent sulfur transfer supplies cysteine; glutathione synthesis requires additional enzymes.
experimental_model
Purified human CTH apo/holo crystal structures and assays
limitations
Purified-enzyme evidence does not define dietary requirements or cellular PLP thresholds.
nutrient_topic
Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B6
organism
Homo sapiens
plain_language
This step releases cysteine for downstream metabolism.
primary_references
[b6-cth-structure-2009] Structural Basis for the Inhibition Mechanism of Human Cystathionine gamma-Lyase, an Enzyme Responsible for the Production of H2S (2009). https://doi.org/10.1074/jbc.M805459200 DOI: 10.1074/jbc.M805459200
tissue_or_cell_type
Purified recombinant protein; no intact tissue
Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 554–564
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human CTH apo/holo crystal structures and assays · source_derived_draft · unverified_draft
### b6-met-cth-cleavage Human CTH cleaves cystathionine to cysteine, 2-oxobutanoate and ammonia in a PLP-dependent reaction. Condition category: normal nutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. plain_language: This step releases cysteine for downstream metabolism. organism: Homo sapiens tissue_or_cell_type: Purified recombinant protein; no intact tissue experimental_model: Purified human CTH apo/holo crystal structures and assays limitations: Purified-enzyme evidence does not define dietary requirements or cellular PLP thresholds. cross_nutrient: B6-dependent sulfur transfer supplies cysteine; glutathione synthesis requires additional enzymes. [b6-cth-structure-2009] Structural Basis for the Inhibition Mechanism of Human Cystathionine gamma-Lyase, an Enzyme Responsible for the Production of H2S (2009). https://doi.org/10.1074/jbc.M805459200 DOI: 10.1074/jbc.M805459200
Complete structured claim and evidence
PLP binds human CTH at Lys212 in an active site assembled from adjacent subunits.
PLP → Human cystathionine gamma-lyase / CTH source_derived_draftungraded
Experimental context and source evidence
cross_nutrient
Second PLP-dependent step of sulfur amino-acid transsulfuration.
evidence_location
Apo, PLP and PLP-PAG structural comparisons
experimental_model
Purified human CTH apo/holo crystal structures and assays
limitations
Purified-enzyme evidence does not define dietary requirements or cellular PLP thresholds.
nutrient_topic
Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B6
organism
Homo sapiens
plain_language
CTH needs an assembled B6-binding catalytic site.
primary_references
[b6-cth-structure-2009] Structural Basis for the Inhibition Mechanism of Human Cystathionine gamma-Lyase, an Enzyme Responsible for the Production of H2S (2009). https://doi.org/10.1074/jbc.M805459200 DOI: 10.1074/jbc.M805459200
tissue_or_cell_type
Purified recombinant protein; no intact tissue
Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 541–552
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human CTH apo/holo crystal structures and assays · source_derived_draft · unverified_draft
### b6-met-cth-plp PLP binds human CTH at Lys212 in an active site assembled from adjacent subunits. Condition category: normal nutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. plain_language: CTH needs an assembled B6-binding catalytic site. organism: Homo sapiens tissue_or_cell_type: Purified recombinant protein; no intact tissue experimental_model: Purified human CTH apo/holo crystal structures and assays limitations: Purified-enzyme evidence does not define dietary requirements or cellular PLP thresholds. cross_nutrient: Second PLP-dependent step of sulfur amino-acid transsulfuration. evidence_location: Apo, PLP and PLP-PAG structural comparisons [b6-cth-structure-2009] Structural Basis for the Inhibition Mechanism of Human Cystathionine gamma-Lyase, an Enzyme Responsible for the Production of H2S (2009). https://doi.org/10.1074/jbc.M805459200 DOI: 10.1074/jbc.M805459200
Complete structured claim and evidence
Human RFK phosphorylates riboflavin to FMN using ATP, yielding ADP; this precedes FLAD1-mediated FAD synthesis.
Riboflavin kinase / RFK → Riboflavin (vitamin B2) source_derived_draftungraded
Experimental context and source evidence
evidence_location
Abstract and product-bound structure
experimental_model
Human RFK structural and catalytic mechanism study
exposure
Purified RFK with flavin and adenine nucleotide ligands.
limitations
Reaction chemistry does not imply RFK controls every tissue flavin pool to the same extent.
nutrient_topic
Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
organism
Homo sapiens
plain_language
RFK performs the first activation step from riboflavin to FMN.
primary_references
[transport-rfk-2003] Ligand binding-induced conformational changes in riboflavin kinase: structural basis for the ordered mechanism. (2003). https://pubmed.ncbi.nlm.nih.gov/14580199/ DOI: 10.1021/bi035450t
tissue_or_cell_type
Purified protein
Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 293–304
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human RFK structural and catalytic mechanism study · source_derived_draft · unverified_draft
### transport-rfk-phosphorylation Human RFK phosphorylates riboflavin to FMN using ATP, yielding ADP; this precedes FLAD1-mediated FAD synthesis. Condition category: normal nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: RFK performs the first activation step from riboflavin to FMN. organism: Homo sapiens tissue_or_cell_type: Purified protein experimental_model: Human RFK structural and catalytic mechanism study limitations: Reaction chemistry does not imply RFK controls every tissue flavin pool to the same extent. exposure: Purified RFK with flavin and adenine nucleotide ligands. evidence_location: Abstract and product-bound structure [transport-rfk-2003] Ligand binding-induced conformational changes in riboflavin kinase: structural basis for the ordered mechanism. (2003). https://pubmed.ncbi.nlm.nih.gov/14580199/ DOI: 10.1021/bi035450t
Complete structured claim and evidence
Human FAD synthase isoform 2 adenylylates FMN with ATP to form FAD and pyrophosphate.
Human FAD synthetase isoform 2 → Flavin mononucleotide source_derived_draftungraded
Experimental context and source evidence
evidence_location
FAD synthesis and reverse pyrophosphorolysis assays
experimental_model
Purified recombinant human FADS2 catalytic assays
exposure
ATP and FMN in FAD-synthesis assays.
limitations
Adenylylation is distinct from RFK phosphorylation; reaction products should not be conflated.
nutrient_topic
Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
organism
Homo sapiens
plain_language
FLAD1 performs the second activation step, making FAD from FMN.
primary_references
[transport-fads2-2011] Human FAD synthase (isoform 2): a component of the machinery that delivers FAD to apo-flavoproteins. (2011). https://pubmed.ncbi.nlm.nih.gov/21951714/ DOI: 10.1111/j.1742-4658.2011.08368.x
tissue_or_cell_type
Purified protein
Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 320–331
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified recombinant human FADS2 catalytic assays · source_derived_draft · unverified_draft
### transport-flad1-adenylylation Human FAD synthase isoform 2 adenylylates FMN with ATP to form FAD and pyrophosphate. Condition category: normal nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: FLAD1 performs the second activation step, making FAD from FMN. organism: Homo sapiens tissue_or_cell_type: Purified protein experimental_model: Purified recombinant human FADS2 catalytic assays limitations: Adenylylation is distinct from RFK phosphorylation; reaction products should not be conflated. exposure: ATP and FMN in FAD-synthesis assays. evidence_location: FAD synthesis and reverse pyrophosphorolysis assays [transport-fads2-2011] Human FAD synthase (isoform 2): a component of the machinery that delivers FAD to apo-flavoproteins. (2011). https://pubmed.ncbi.nlm.nih.gov/21951714/ DOI: 10.1111/j.1742-4658.2011.08368.x
Complete structured claim and evidence
Recombinant human FLAD1 isoforms 1 and 2 exhibited FAD synthetase activity; isoform 2 was purified, and activity required MgCl2.
Human FAD synthetase isoform 2 → FAD source_derived_draftungraded
Experimental context and source evidence
cross_nutrient
B2 activation and Mg-dependent FAD synthesis provide a biochemical partner to B1-dependent complexes; direct transfer of newly made FAD to DLD was not tested.
evidence
[{"paper_key": "brizio-2006-fad", "source_bundle": "artifacts/thiamine_metabolism_sources.json", "passage_ids": ["abstract"], "locator": "Primary publication abstract", "preservation": "Exact text retained in the source bundle; full source document retained when openly retrievable."}]
experimental_model
Recombinant human FLAD1 isoforms expressed in E. coli.
limitations
No tissue Mg threshold or combined B1/B2 deficiency experiment.
nutrient
Thiamine (vitamin B1) · Thiamine (vitamin B1)
nutrient_topic
Thiamine research collection; topical membership is not evidence of a direct dietary effect. · Thiamine (vitamin B1)
organism
Homo sapiens
plain_language
The flavin used by E3 must first be made from the riboflavin pathway. This distinct magnesium-dependent synthesis reaction should not be confused with magnesium binding to B1 enzymes.
primary_references
[brizio-2006-fad] Over-expression in Escherichia coli and characterization of two recombinant isoforms of human FAD synthetase (2006). https://pubmed.ncbi.nlm.nih.gov/16643857/ DOI: 10.1016/j.bbrc.2006.04.003
tissue_or_cell_type
Purified/expressed proteins
Thiamine: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 745–757
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human FLAD1 isoforms expressed in E. coli. · source_derived_draft · unverified_draft
### b1-fad-b2-cofactor-synthesis Recombinant human FLAD1 isoforms 1 and 2 exhibited FAD synthetase activity; isoform 2 was purified, and activity required MgCl2. Condition category: normal nutrient_topic: Thiamine research collection; topical membership is not evidence of a direct dietary effect. plain_language: The flavin used by E3 must first be made from the riboflavin pathway. This distinct magnesium-dependent synthesis reaction should not be confused with magnesium binding to B1 enzymes. organism: Homo sapiens tissue_or_cell_type: Purified/expressed proteins experimental_model: Recombinant human FLAD1 isoforms expressed in E. coli. limitations: No tissue Mg threshold or combined B1/B2 deficiency experiment. evidence: [{"paper_key": "brizio-2006-fad", "source_bundle": "artifacts/thiamine_metabolism_sources.json", "passage_ids": ["abstract"], "locator": "Primary publication abstract", "preservation": "Exact text retained in the source bundle; full source document retained when openly retrievable."}] cross_nutrient: B2 activation and Mg-dependent FAD synthesis provide a biochemical partner to B1-dependent complexes; direct transfer of newly made FAD to DLD was not tested. nutrient: Thiamine (vitamin B1) [brizio-2006-fad] Over-expression in Escherichia coli and characterization of two recombinant isoforms of human FAD synthetase (2006). https://pubmed.ncbi.nlm.nih.gov/16643857/ DOI: 10.1016/j.bbrc.2006.04.003
Complete structured claim and evidence

Availability and dependencies

Each situation shows the normal role first, then what the sources report under a specific condition. A shortfall in the diet, a fault in the machinery, and a low blood reading are kept separate because they are not the same thing.

Low intake slows molybdenum loss

Condition: nutrient_deficiency · Controlled low intake for 102 days

Normal role: Absorbed molybdenum is retained or excreted.

Recorded consequence: Balance improved over time and turnover slowed; overt deficiency signs were not observed.

Scope: Four healthy young men

A fault in scaffold construction blocks cofactor production

Condition: machinery_impairment · Patient-derived MOCS2 mutations

Normal role: MOCS2 subunits bind each other and convert cPMP to MPT.

Recorded consequence: Weaker subunit association or impaired precursor binding reduces MPT-synthase function.

Scope: Recombinant human patient variants

Cofactor sulfur activation can fail despite mineral supply

Condition: machinery_impairment · MOCOS patient variants

Normal role: MOCOS provides terminal sulfur for XDH and AOX1.

Recorded consequence: Defects affect PLP-dependent sulfur mobilization or cofactor binding, producing type II xanthinuria.

Scope: Human MOCOS domain biochemistry and patient genetics

An enzyme can work in a test tube but fail to mature in cells

Condition: machinery_impairment · SUOX Gly362Ser variant

Normal role: SUOX must bind Moco and complete mitochondrial maturation.

Recorded consequence: Cofactor insertion and cellular activity are impaired despite activity of bacterially expressed protein.

Scope: Patient fibroblasts and recombinant human protein

Without the cofactor, SUOX may fail to stay in mitochondria

Condition: machinery_impairment · Loss of Moco availability during maturation

Normal role: Imported SUOX binds Moco, is retained, then loads heme and dimerizes.

Recorded consequence: Processed enzyme accumulates in cytosol and later maturation steps fail.

Scope: Mammalian SUOX maturation experiments

Loss of sulfite clearance changes other sulfur pools

Condition: machinery_impairment · SUOX deletion in human cells

Normal role: Sulfite from cysteine catabolism is oxidized to sulfate.

Recorded consequence: Sulfite, H2S and persulfidated metabolites accumulate alongside altered SQOR abundance.

Scope: Human HEK293T knockout models

An AOX1 variant fails to carry its molybdenum cofactor

Condition: machinery_impairment · AOX1 Gly1269Arg variant

Normal role: AOX1 must assemble Moco and its other redox cofactors.

Recorded consequence: The purified protein was inactive and its crystal lacked Moco.

Scope: Recombinant human AOX1 structure

A wrong metal or damaged binding site disables this mARC reaction

Condition: machinery_impairment · Tungsten substitution or Cys273Ala mutation

Normal role: Moco-loaded mARC can reduce nitrite.

Recorded consequence: The tested enzyme lost measurable NO-forming activity.

Scope: Recombinant human mARC1

An acquired shortage can impair both sulfur and purine handling

Condition: nutrient_deficiency · Prolonged total parenteral nutrition in the reported patient

Normal role: Moco-dependent SUOX and XDH process sulfite and purine metabolites.

Recorded consequence: Amino-acid intolerance and sulfur/purine abnormalities improved after ammonium molybdate.

Scope: One human case; not the usual dietary setting

A cofactor assembly defect affects more than one enzyme

Condition: machinery_impairment · Inherited MoCD type A or B

Normal role: MOCS proteins build Moco before enzymes can use molybdenum.

Recorded consequence: Sulfite-related and purine metabolites accumulate; severe neurological disease is common.

Scope: Human genetically defined MoCD

Replacement works only if the remaining assembly steps function

Condition: machinery_impairment · MOCS1/type A or downstream MOCS2/type B defects

Normal role: MOCS1 makes cPMP, which downstream enzymes convert into Moco.

Recorded consequence: cPMP corrected markers in type A but not type B in this cohort.

Scope: Human neonatal MoCD cohort

One enzyme can fail while other molybdenum pathways remain intact

Condition: machinery_impairment · Inherited XDH defects

Normal role: XDH supports purine breakdown to urate.

Recorded consequence: Classical type I xanthinuria results from XDH loss.

Scope: Human patient genetics

Failed sulfite clearance can trigger a neuronal calcium cascade

Condition: machinery_impairment · MoCD-model sulfite accumulation and SSC exposure

Normal role: SUOX oxidizes sulfite before excessive reactive sulfur metabolites accumulate.

Recorded consequence: SSC activates excitatory receptors, increases calcium and calpain activity, and destabilizes inhibitory synapses.

Scope: Chemical reactions, primary mouse neurons and tungstate-treated mice

Sulfite can impair glutamate-supported energy production

Condition: machinery_impairment · Sulfite exposure to rat mitochondrial preparations

Normal role: GDH supplies reducing equivalents during glutamate oxidation.

Recorded consequence: GDH activity, glutamate-driven NADH, membrane potential and ATP generation declined.

Scope: Rat brain mitochondria and rodent cells

Sulfite effects on glutathione and enzymes change with time

Condition: machinery_impairment · Sulfite exposure in rat cortex slices

Normal role: Glutamate transport and antioxidant systems maintain neural homeostasis.

Recorded consequence: Transport and glutathione changed before several enzyme activities fell.

Scope: Rat cortical slices; one- and three-hour assays

Loss of sulfite oxidation changes mitochondrial function and shape

Condition: machinery_impairment · Mouse SO deletion or patient MoCD; experimental sulfite elevation

Normal role: SUOX prevents excess sulfite accumulation.

Recorded consequence: ATP support was impaired and network interconnection or fragmentation depended on conditions.

Scope: Mouse and human fibroblast experiments

An MTARC1 variant changes protein location and stability

Condition: machinery_impairment · A165T knock-in in HepG2 cells

Normal role: MTARC1 is anchored at the outer mitochondrial membrane.

Recorded consequence: Mislocalization, faster degradation and lower N-reduction occurred.

Scope: Human hepatoma-cell model

Does losing MTARC1 protect the liver? Published mouse results differ

Condition: machinery_impairment · Experimental global or liver-specific Mtarc1 loss

Normal role: MTARC1 supports redox reactions; its link to liver fat is under investigation.

Recorded consequence: Some studies report protection, while another did not; candidate explanations remain open.

Scope: Distinct mouse disease models, with human genetic context

The sources

Every document behind this chapter is preserved word for word. Open one to read it in full with its recorded conflicts marked in place.

Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source
Pantothenic acid (vitamin B5): coenzyme A, deficiency and nutrient interactions (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source
Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source
Thiamine: mechanisms, deficiency and nutrient interactions (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source
Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source

Recorded disagreements

Where two sources say different things, both are kept and the difference is explained. You can discuss a disagreement or propose a mechanism that might account for it.

MTARC1 knockout: conflicting liver-protection results in miceA 2024 whole-body knockout study reported no protection against triglyceride accumulation, inflammation or fibrosis; 2025 and 2026 studies reported protection after global deletion and liver-directed interventions. Genetic background, diet, disease induction, timing, sex and Marc2 contribution are candidate explanations that require direct comparison. The A168T knock-in is a different perturbation and is retained as context rather than labeled the same experiment.Read the recorded disagreement

Open questions in this collection

Questions the curators could not answer from the sources in front of them, kept here with the reason each one is still open. These are gaps in this collection, not findings or proof that no one has studied them.

Which physiological conditions make sulfur supply limiting between MOCS3-dependent Moco synthesis and URM1-dependent RNA thiolation?A shared protein is established; a competition hierarchy or human dietary bottleneck has not been established by the cited studies.
Does clinically common B6, iron or magnesium deficiency measurably reduce specific human Moco-enzyme activities?PLP-dependent sulfur mobilization, Fe-S clusters and ATP-dependent assembly provide biochemical connections. Their existence does not establish that supplementing one nutrient rescues another in every person.
How is cPMP exported from human mitochondria?Human MOCS1 targeting is established. Plant ATM3/ABCB7 analogies are not sufficient to assign a proven human cPMP exporter.
What explains the incompatible whole-body Mtarc1 knockout liver outcomes?Direct comparisons of genetic background, paralogs, diet, sex, duration and lipid-droplet mechanisms are needed. Human genetic associations do not resolve all mouse-model differences.
How does human MTARC1 activity regulate liver lipids, and which substrates matter?N-reduction and nitrite reduction are established capabilities; a complete causal human substrate-to-lipid pathway and clinical benefit from targeted inhibition remain unsettled.
At what human exposures does dietary molybdate alter copper status?Sheep-rumen thiomolybdates, yeast copper-chaperone experiments and therapeutic tetrathiomolybdate are different forms and contexts; they cannot define an ordinary dietary antagonism threshold.
Which downstream neurological mechanisms can be therapeutically modified in human MoCD?SSC/NMDA/calcium/calpain and mitochondrial routes have model support. Mouse memantine rescue is not proof of patient benefit, and prenatal injury may limit postnatal rescue.
How much do SUOX, XOR and mARC contribute to NO production at physiological substrate levels in specific human tissues?Purified-enzyme rates, engineered expression and artificial mediators do not establish their quantitative importance in vivo.
Does molybdenum supplementation improve sulfite sensitivity, yeast-related symptoms, histamine intolerance or acetaldehyde clearance in otherwise replete people?The cited enzyme chemistry does not demonstrate these clinical treatment claims. AOX1 is not interchangeable with alcohol-metabolizing ALDH enzymes.
Can sulfite accumulation cause clinically important thiamine destruction in humans at documented tissue concentrations?Chemical sulfite-thiamine reactions and food preservation studies do not by themselves establish a human B1-repletion failure syndrome caused by ordinary molybdenum shortage.
Which transporters dominate molybdate uptake and retention in each human tissue?MFSD5 has demonstrated transport capacity, but partial knockdown did not suppress uptake in HEK-293T cells. Capacity and physiological necessity are distinct; these results are not opposing transport directions.
What measurements identify clinically meaningful intracellular molybdenum shortage in ordinary populations?Small balance studies measure adaptation, not universal enzyme-occupancy or disease thresholds. Plasma molybdenum alone does not resolve intracellular Moco availability.

Chapters are assembled from supplied drafts and curated literature summaries. Statements remain unverified against the primary studies, and the ledger is not medical advice.

Evidence, AI assistance and curation standards

Molybdenum

The mechanisms

Human sulfite oxidase converts sulfite to sulfate in the terminal oxidative step of cysteine catabolism.

Recombinant human XDH/XOR catalyzed conversion of xanthine to urate.

Human AOX1 structures and kinetics characterize phthalazine binding and oxidation at its molybdenum active site.

Recombinant human mARC1 reduced N-hydroxylated compounds, including N-hydroxycytosine.

Recombinant human mARC2 also reduced N-hydroxylated substrates, with specificity differing from mARC1.

MOCS1A and MOCS1B jointly support conversion of GTP to cPMP, the first intermediate of human Moco synthesis.

Human NFS1 transferred sulfur from L-cysteine through an NFS1-bound persulfide intermediate to the rhodanese-like domain of MOCS3.

MOCS3 activates MOCS2A by adenylation followed by sulfur transfer, forming its C-terminal thiocarboxylate.

Human MOCS2A and MOCS2B assemble as active MPT synthase and convert cPMP to molybdopterin.

The gephyrin G domain produces adenylylated molybdopterin.

The gephyrin E domain catalyzes molybdate incorporation during ATP-dependent Moco synthesis.

MOCOS defects in type II xanthinuria support its role in supplying the terminal sulfur required by XDH and AOX1.

Measured molybdenum absorption was 88-93% across the five controlled dietary intakes.

Both the amount and percentage of molybdenum excreted in urine rose with dietary intake.

At 22 micrograms/day, molybdenum turnover slowed and balance improved with time, although balance was not consistently achieved.

No clinical signs of molybdenum deficiency were observed during the 102-day low-intake phase.

Modeled fractional tissue storage was lower during repletion than during depletion, while urinary elimination increased.

The compartmental model estimated food-bound molybdenum to be approximately 16% less bioavailable than purified molybdenum.

Human HsMOT2/MFSD5 expression supported molybdate uptake in yeast, with an apparent affinity near 550 nM.

Tungstate inhibited HsMOT2-dependent molybdate uptake in yeast; 1 mM sulfate had little effect.

Large HsMOT2/MFSD5 overexpression increased the molybdate-sensitive FRET signal in HEK-293T cells.

Reducing MFSD5 mRNA to 11-35% of control did not reduce molybdate uptake signals at the tested doses.

Oxalate at 10 mM inhibited molybdate accumulation in HEK-293T cells.

Adding 1 mM sulfate had little effect on HEK-293T molybdate uptake signals.

Exon 1a targeted type I MOCS1A to the mitochondrial matrix, whereas exon 1b variants remained cytosolic.

MOCS1AB fusion precursors underwent mitochondrial import and proteolytic cleavage that released the matrix-localized MOCS1B domain.

Anaerobic reconstitution yielded human MOCS1A containing two [4Fe-4S] clusters.

MOCS1A contains a redox-active N-terminal [4Fe-4S] cluster coordinated by the conserved radical-SAM cysteine motif.

Oxygen rapidly degraded both reconstituted MOCS1A [4Fe-4S] clusters, producing different semistable cluster intermediates.

Purified NFS1 interacted specifically with MOCS3-RLD and supported sulfur transfer to it.

FRET and split-EGFP supported an NFS1-MOCS3 interaction in the cytosol of human cells.

The sulfur used to form the MPT dithiolene group is supplied from the C-terminal thiocarboxylate of the small MPT-synthase subunit.

MOCS2A Val7Phe weakened its interaction with MOCS2B in reconstituted human MPT synthase.

MOCS2B Glu168Lys attenuated binding of precursor Z/cPMP.

MOCS3 also activates URM1 by adenylation and sulfur transfer to its terminal glycine.

Removing the terminal glycine from MOCS2A or URM1 abolished the measured interaction with MOCS3.

Full gephyrin supported over 300-fold greater Moco synthesis than the separated G and E domains in the reported reconstitution system.

The purified human MOCOS NifS-like domain bound PLP and exhibited cysteine desulfurase activity.

The Thr349Ile MOCOS N-terminal domain had severely impaired cysteine desulfurase activity, including a preparation with measurable PLP binding.

MOCOS Pro591Ser impaired cofactor binding in the C-terminal domain assay.

MOCOS Arg776Cys impaired cofactor binding in the C-terminal domain assay.

SUOX sulfite oxidation depends on Moco at the catalytic site and a separate heme cofactor.

Apo-G362S SUOX reconstituted with Moco about 90-fold less efficiently than wild type; patient fibroblasts had no detectable activity.

Adding molybdate to culture medium partially rescued Moco binding and restored detectable SUOX activity in the G362S patient fibroblasts.

Moco binding was required for mitochondrial trapping and retention of processed sulfite oxidase.

Heme binding occurred only after Moco integration in the studied SUOX maturation pathway.

SUOX dimerization did not occur in the absence of Moco and followed cofactor insertion.

Human CDO1 oxidizes cysteine to cysteine sulfinic acid using molecular oxygen and a non-heme iron center.

GOT1 was the principal contributor to cysteine-sulfinate conversion to sulfite and pyruvate in the studied human-cell system.

SUOX deficiency was accompanied by increased H2S steady-state levels without upregulation of the known H2S-producing pathways.

SUOX-deficient cells accumulated persulfidated glutathione and cysteine.

The sulfite-accumulating cells had increased SQOR protein levels.

The primary article describes sequential XOR hydroxylation of hypoxanthine to xanthine and xanthine to urate.

The XDH form transfers purine-derived electrons through its iron-sulfur centers and FAD to NAD+, producing NADH.

In its oxidase activity, XOR can generate superoxide and hydrogen peroxide rather than exclusively transferring electrons to NAD+.

Human XOR reduced nitrite to NO under the tested reducing conditions, and nitrite decreased XOR-driven superoxide production.

His1221Arg increased urate, superoxide and NO formation relative to wild type in xanthine-supplied assays.

Ile703Val increased urate and NO formation without increasing superoxide formation in the reported comparison.

Thioridazine bound a distinct noncompetitive inhibitor site in human AOX1.

AOX1-bound FAD acted as the intrinsic fluorescence reporter in ThermoFAD unfolding assays.

The inactive AOX1 G1269R crystal structure lacked the entire Moco cofactor.

A separable aldehyde-oxidase fraction accounted for some NAD-independent retinaldehyde metabolism in human liver and kidney extracts.

Recombinant human AOX converted all-trans-retinaldehyde to all-trans-retinoic acid, with an apparent Km near 1.5 micromolar.

In human liver S9, AOX inhibition reduced retinoic-acid formation by 20-50%, versus 50-80% with ALDH1A1 inhibition; AOX had lower affinity and higher capacity.

Inhibitor and fractionation experiments implicated AO and carboxylesterase, but not XOR, in GDC-0834 amide hydrolysis.

The reconstituted mARC system used NADH/FAD-dependent cytochrome b5 reductase and heme-containing cytochrome b5.

Active mARC1 and mARC2 were reconstituted with Moco without the terminal sulfuration needed by the XOR enzyme family.

Mitochondrial CYB5B was required for the mARC-containing N-reductive system in the studied human cells.

Heme-free apo-CYB5 failed to support N-reduction in the reconstituted system.

CYB5A siRNA in HEK293 cells and Cyb5a knockout in mice did not support a required role for the microsomal isoform in measured N-reduction.

Reduced human mARC1 generated nitric oxide from nitrite in the reconstituted electron-transfer chain.

Reduced human mARC2 also catalyzed nitrite-to-NO conversion.

Lowering assay pH from 7.5 to 6.5 increased the reported mARC NO-formation rate by nearly threefold.

The C273A mARC1 variant abolished nitrite-dependent NO formation.

Replacing molybdenum with tungsten during recombinant mARC1 production abolished NO formation.

Human SUOX reduced nitrite to NO at the molybdenum center, with steady-state turnover supported in a sulfite/cytochrome-c system.

Electrochemical human SUOX nitrite reduction had a reported Km of 3.5 mM at pH 7; a heme-free variant behaved similarly in that system.

The prolonged-TPN case developed amino-acid intolerance with high plasma methionine, high urinary sulfite/thiosulfate and low urinary sulfate.