[2Fe-2S] iron-sulfur cluster

cross_nutrient

B6 and iron-sulfur cluster coexistence; functional nutritional interaction remains untested.

experimental_model

Pig liver GABA aminotransferase; inhibitor complexes and spectroscopy

exposure

Native and inhibitor-bound enzyme crystallography.

limitations

The cluster function was unknown; no iron-deficiency or B6-rescue response was demonstrated.

nutrient_topic

Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B6

organism

Sus scrofa

plain_language

Iron and B6 occur in the same enzyme structure.

primary_references

[storici-2004-gaba-at] Structures of gamma-aminobutyric acid (GABA) aminotransferase, a pyridoxal 5'-phosphate, and [2Fe-2S] cluster-containing enzyme, complexed with gamma-ethynyl-GABA and with the antiepilepsy drug vigabatrin (2004). https://doi.org/10.1074/jbc.M305884200 DOI: 10.1074/jbc.M305884200

tissue_or_cell_type

Pig liver enzyme

Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1083–1094

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Pig liver GABA aminotransferase; inhibitor complexes and spectroscopy · source_derived_draft · unverified_draft

### b6-neuro-gaba-at-iron-cluster Native and inhibitor-bound pig liver GABA-AT structures resolved a [2Fe-2S] cluster near the PLP sites. Condition category: normal nutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Iron and B6 occur in the same enzyme structure. organism: Sus scrofa tissue_or_cell_type: Pig liver enzyme experimental_model: Pig liver GABA aminotransferase; inhibitor complexes and spectroscopy limitations: The cluster function was unknown; no iron-deficiency or B6-rescue response was demonstrated. exposure: Native and inhibitor-bound enzyme crystallography. cross_nutrient: B6 and iron-sulfur cluster coexistence; functional nutritional interaction remains untested. [storici-2004-gaba-at] Structures of gamma-aminobutyric acid (GABA) aminotransferase, a pyridoxal 5'-phosphate, and [2Fe-2S] cluster-containing enzyme, complexed with gamma-ethynyl-GABA and with the antiepilepsy drug vigabatrin (2004). https://doi.org/10.1074/jbc.M305884200 DOI: 10.1074/jbc.M305884200

evidence_span

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experimental_model

Purified reconstructed COQ metabolon with short-chain substrates

exposure

Enzyme combinations, methyl donors, reductants and metal additions

limitations

Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species.

nutrient_topic

Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system

organism

Reconstructed ancestral tetrapod proteins

plain_language

Iron participates in an electron-transfer component, not as a substitute for CoQ.

primary_references

[coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z

tissue_or_cell_type

Stepwise CoQ head-group assembly

Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 606–617

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified reconstructed COQ metabolon with short-chain substrates · source_derived_draft · unverified_draft

### coq10-fdx2-iron Purified reconstructed FDX2 retained a two-iron, two-sulfur cluster. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Iron participates in an electron-transfer component, not as a substitute for CoQ. organism: Reconstructed ancestral tetrapod proteins tissue_or_cell_type: Stepwise CoQ head-group assembly experimental_model: Purified reconstructed COQ metabolon with short-chain substrates limitations: Ancestral proteins and CoQ1 analogues; no clinical cofactor dose or proof of nutritional rate limitation. Reaction order need not be universal across species. exposure: Enzyme combinations, methyl donors, reductants and metal additions evidence_span: {"source_cache": "artifacts/coq10-research/38425362.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7d25af4ecd7340649536b8fea3b8a0a308a1611bbf8c57f6a79b362f443f1cba", "start_char": 9067, "end_char": 13813, "text_sha256": "49612ae4d3a59a75a02fe3fb132abd8aeb7ef8b7cae3b0f79b5557503c55ad51"} [coq10-p38425362] In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. (2024). https://pubmed.ncbi.nlm.nih.gov/38425362/ DOI: 10.1038/s41929-023-01087-z

evidence_span

{"source_cache": "artifacts/iron-research/11175906.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ba1c88d4630f6f0ee7f70989705c81162a2f8651c066f46b3aac73988b8dfa11", "start_char": 0, "end_char": 770, "text_sha256": "ba1c88d4630f6f0ee7f70989705c81162a2f8651c066f46b3aac73988b8dfa11"}

experimental_model

Human ferrochelatase crystal structure

exposure

2.0 angstrom structure and biochemical catalytic interpretation

limitations

Purified enzyme; cluster structure is not a human dietary-iron threshold.

nutrient_topic

Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron

organism

Human enzyme

plain_language

The enzyme that inserts iron also carries its own iron-sulfur cofactors.

primary_references

[iron-p11175906] The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis. (2001). https://pubmed.ncbi.nlm.nih.gov/11175906/ DOI: 10.1038/84152

tissue_or_cell_type

Mitochondrial membrane-associated enzyme

Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 524–535

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human ferrochelatase crystal structure · source_derived_draft · unverified_draft

### iron-fech-clusters The human ferrochelatase homodimer contained two uniquely coordinated, nitric-oxide-sensitive [2Fe-2S] clusters. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: The enzyme that inserts iron also carries its own iron-sulfur cofactors. organism: Human enzyme tissue_or_cell_type: Mitochondrial membrane-associated enzyme experimental_model: Human ferrochelatase crystal structure limitations: Purified enzyme; cluster structure is not a human dietary-iron threshold. exposure: 2.0 angstrom structure and biochemical catalytic interpretation evidence_span: {"source_cache": "artifacts/iron-research/11175906.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ba1c88d4630f6f0ee7f70989705c81162a2f8651c066f46b3aac73988b8dfa11", "start_char": 0, "end_char": 770, "text_sha256": "ba1c88d4630f6f0ee7f70989705c81162a2f8651c066f46b3aac73988b8dfa11"} [iron-p11175906] The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis. (2001). https://pubmed.ncbi.nlm.nih.gov/11175906/ DOI: 10.1038/84152

cross_nutrient

true

evidence_location

Primary Tables 3-5, Figure 6A and Experimental procedures; full text retrieved.

experimental_model

Human CYP27B1/FDX1/FDXR kinetic reconstitution

exposure

FDX1 1-30 micromolar; 2-min incubations with calcifediol; Table 4.

limitations

The experiment varies intact FDX1, not dietary iron. Reciprocal changes of apparent Km and turnover prevent interpreting FDX1 level as a universal limiting factor.

nutrient

Vitamin D2 and D3 · Vitamin D2 and D3

nutrient_topic

Vitamin D2 and D3 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin D2 and D3

organism

Homo sapiens proteins

plain_language

An iron-sulfur electron carrier supports the final D3 activation step.

primary_references

[tang2012] Expression of human CYP27B1 in Escherichia coli and characterization in phospholipid vesicles. (2012). https://pubmed.ncbi.nlm.nih.gov/22862690/ DOI: 10.1111/j.1742-4658.2012.08736.x

tissue_or_cell_type

reconstituted mitochondrial membrane

Vitamin D2 and D3: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 452–465

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human CYP27B1/FDX1/FDXR kinetic reconstitution · source_derived_draft · unverified_draft

### vd-act-fdx1-cyp27b1 Human adrenodoxin supported CYP27B1 activity in reconstituted vesicles; varying adrenodoxin changed apparent kinetic parameters for calcifediol hydroxylation. Condition category: normal nutrient_topic: Vitamin D2 and D3 research collection; topical membership is not evidence of a direct dietary effect. plain_language: An iron-sulfur electron carrier supports the final D3 activation step. organism: Homo sapiens proteins tissue_or_cell_type: reconstituted mitochondrial membrane experimental_model: Human CYP27B1/FDX1/FDXR kinetic reconstitution limitations: The experiment varies intact FDX1, not dietary iron. Reciprocal changes of apparent Km and turnover prevent interpreting FDX1 level as a universal limiting factor. exposure: FDX1 1-30 micromolar; 2-min incubations with calcifediol; Table 4. cross_nutrient: true evidence_location: Primary Tables 3-5, Figure 6A and Experimental procedures; full text retrieved. nutrient: Vitamin D2 and D3 [tang2012] Expression of human CYP27B1 in Escherichia coli and characterization in phospholipid vesicles. (2012). https://pubmed.ncbi.nlm.nih.gov/22862690/ DOI: 10.1111/j.1742-4658.2012.08736.x

evidence_access

Primary full text

experimental_model

Purified soluble cytosolic domain, residues 32–108.

limitations

Association does not demonstrate altered iron-sulfur transfer or clinical mitochondrial benefit.

nutrient_topic

Resveratrol collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Resveratrol

plain_language

The sulfate metabolite has a target the parent did not share.

primary_references

Complexes of the outer mitochondrial membrane protein mitoNEET with resveratrol-3-sulfate. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21591687/ · DOI 10.1021/bi200546s

Resveratrol: metabolites, target selectivity and cross-nutrient mechanisms (2026-09-19) · lines 126–132

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified soluble cytosolic domain, residues 32–108. · source_derived_draft · unverified_draft

## resveratrol-mitoneet-metabolite The sulfate metabolite has a target the parent did not share. Resveratrol-3-sulfate associated with the soluble human mitoNEET domain in mass-spectrometry and calorimetry experiments, with fitted dissociation constants approximately 5–16 micromolar. Model: Purified soluble cytosolic domain, residues 32–108. Limitations: Association does not demonstrate altered iron-sulfur transfer or clinical mitochondrial benefit. Evidence access: Primary full text Complexes of the outer mitochondrial membrane protein mitoNEET with resveratrol-3-sulfate. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21591687/ · DOI 10.1021/bi200546s

cross_nutrient

B2-derived FAD and iron-containing redox centers cooperate within one respiratory complex.

evidence_spans

[{"source_bundle": "artifacts/riboflavin_metabolism_sources.json", "source_key": "PMC10161127", "locator": "XML .//body//p", "paragraph_index": 2, "char_start": 0, "char_end": 1105, "evidence_access": "full-text"}]

experimental_model

Human complex II purified from HEK293F cells, cryo-EM, EPR and succinate-quinone activity assays.

exposure

No nutrient intervention; structural or biochemical characterization.

limitations

Structural co-dependence does not show that B2 corrects iron deficiency or that iron supplementation improves this reaction.

nutrient_topic

Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)

organism

Homo sapiens

plain_language

Complex II couples a B2-derived flavin with separate iron-sulfur centers.

primary_references

[du-2023-human-complex-ii] Structure of the human respiratory complex II (2023). https://pubmed.ncbi.nlm.nih.gov/37098072/ DOI: 10.1073/pnas.2216713120

tissue_or_cell_type

HEK293F-derived purified complex II

Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 649–661

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human complex II purified from HEK293F cells, cryo-EM, EPR and succinate-quinone activity assays. · source_derived_draft · unverified_draft

### b2-met-human-sdhb-iron-sulfur Human complex II structure and EPR resolved SDHB-associated [2Fe-2S], [4Fe-4S] and [3Fe-4S] redox centers adjacent to its SDHA FAD system. Condition category: normal nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Complex II couples a B2-derived flavin with separate iron-sulfur centers. organism: Homo sapiens tissue_or_cell_type: HEK293F-derived purified complex II experimental_model: Human complex II purified from HEK293F cells, cryo-EM, EPR and succinate-quinone activity assays. limitations: Structural co-dependence does not show that B2 corrects iron deficiency or that iron supplementation improves this reaction. exposure: No nutrient intervention; structural or biochemical characterization. cross_nutrient: B2-derived FAD and iron-containing redox centers cooperate within one respiratory complex. evidence_spans: [{"source_bundle": "artifacts/riboflavin_metabolism_sources.json", "source_key": "PMC10161127", "locator": "XML .//body//p", "paragraph_index": 2, "char_start": 0, "char_end": 1105, "evidence_access": "full-text"}] [du-2023-human-complex-ii] Structure of the human respiratory complex II (2023). https://pubmed.ncbi.nlm.nih.gov/37098072/ DOI: 10.1073/pnas.2216713120

evidence_span

{"source_cache": "artifacts/ala-research/33562493.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4261f63098ce640cc87368d3f23f294441fdfa2a3f9b271086821fc1196bb3ac", "start_char": 0, "end_char": 1544, "text_sha256": "4261f63098ce640cc87368d3f23f294441fdfa2a3f9b271086821fc1196bb3ac"}

experimental_model

Recombinant human LIAS cluster reconstitution, EPR and LC-MS

exposure

[2Fe-2S]-loaded ISCU or ISCA2 donors

limitations

In vitro donor capacity does not establish a unique physiological donor or exclude other routes.

nutrient_topic

Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. · Lipoic acid

organism

Human proteins

plain_language

These carrier proteins can help rebuild active enzyme under assay conditions.

primary_references

[ala-p33562493] Characterization and Reconstitution of Human Lipoyl Synthase (LIAS) Supports ISCA2 and ISCU as Primary Cluster Donors and an Ordered Mechanism of Cluster Assembly. (2021). https://pubmed.ncbi.nlm.nih.gov/33562493/ DOI: 10.3390/ijms22041598

tissue_or_cell_type

Two LIAS iron-sulfur sites

Alpha-lipoic acid: cofactor assembly, redox signaling and nutrient interactions (2026-09-17) · lines 390–401

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human LIAS cluster reconstitution, EPR and LC-MS · source_derived_draft · unverified_draft

### ala-iscu-isca2-reconstitution [2Fe-2S]-loaded human ISCU and ISCA2 reconstituted catalytically active human LIAS in vitro. Condition category: normal nutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: These carrier proteins can help rebuild active enzyme under assay conditions. organism: Human proteins tissue_or_cell_type: Two LIAS iron-sulfur sites experimental_model: Recombinant human LIAS cluster reconstitution, EPR and LC-MS limitations: In vitro donor capacity does not establish a unique physiological donor or exclude other routes. exposure: [2Fe-2S]-loaded ISCU or ISCA2 donors evidence_span: {"source_cache": "artifacts/ala-research/33562493.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4261f63098ce640cc87368d3f23f294441fdfa2a3f9b271086821fc1196bb3ac", "start_char": 0, "end_char": 1544, "text_sha256": "4261f63098ce640cc87368d3f23f294441fdfa2a3f9b271086821fc1196bb3ac"} [ala-p33562493] Characterization and Reconstitution of Human Lipoyl Synthase (LIAS) Supports ISCA2 and ISCU as Primary Cluster Donors and an Ordered Mechanism of Cluster Assembly. (2021). https://pubmed.ncbi.nlm.nih.gov/33562493/ DOI: 10.3390/ijms22041598

cross_nutrient

true

evidence_location

Abstract and indexed primary Results, Figure 3

experimental_model

Purified human proteins

exposure

FDX1, FDXR and NADPH with MMAB, cob(II)alamin and ATP

limitations

Biochemically competent donor; exclusivity or necessity in living humans was not tested.

nutrient_topic

Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B12 (cobalamins)

organism

Homo sapiens

plain_language

In the purified human system, an iron-sulfur electron carrier supported B12 activation.

primary_references

[gouda-2023-mmab-redox] Coordination Chemistry Controls Coenzyme B12 Synthesis by Human Adenosine Triphosphate:Cob(I)alamin Adenosyltransferase. (2023). https://pubmed.ncbi.nlm.nih.gov/37526260/ DOI: 10.1021/acs.inorgchem.3c02163

tissue_or_cell_type

Purified protein assay

Vitamin B12: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1005–1017

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human proteins · source_derived_draft · unverified_draft

### fdx1-supports-mmab Human [2Fe-2S] ferredoxin FDX1 supplied electrons for MMAB-dependent adenosylcobalamin synthesis in the FDXR/NADPH reconstitution. Condition category: normal nutrient_topic: Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. plain_language: In the purified human system, an iron-sulfur electron carrier supported B12 activation. organism: Homo sapiens tissue_or_cell_type: Purified protein assay experimental_model: Purified human proteins limitations: Biochemically competent donor; exclusivity or necessity in living humans was not tested. exposure: FDX1, FDXR and NADPH with MMAB, cob(II)alamin and ATP cross_nutrient: true evidence_location: Abstract and indexed primary Results, Figure 3 [gouda-2023-mmab-redox] Coordination Chemistry Controls Coenzyme B12 Synthesis by Human Adenosine Triphosphate:Cob(I)alamin Adenosyltransferase. (2023). https://pubmed.ncbi.nlm.nih.gov/37526260/ DOI: 10.1021/acs.inorgchem.3c02163

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

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