Molybdenum cofactor / Moco

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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