{"id":"b46ff655-62aa-53de-85a6-c53c381a5c2b","stable_key":"dc8975b1-95ff-5d9b-be17-a1c04610cca7:mo-xdh-nad","predicate":"transfers_electrons_to","statement":"The XDH form transfers purine-derived electrons through its iron-sulfur centers and FAD to NAD+, producing NADH.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"dca91016-4d79-5c6a-8d6d-2822e66c23c8","mechanism_event_label":"Riboflavin-derived FAD, iron-sulfur centers and niacin-derived NAD work alongside molybdenum.","subject":{"id":"8de34d8a-46dc-512c-a82f-d169747b496e","slug":"xdh","display_name":"Human xanthine oxidoreductase / XDH","entity_type_key":"protein"},"object":{"id":"283ed24b-06a1-50aa-9281-df3bac6ce37e","slug":"nad-plus","display_name":"NAD+","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"dca91016-4d79-5c6a-8d6d-2822e66c23c8","stable_key":"dc8975b1-95ff-5d9b-be17-a1c04610cca7:mo-xdh-nad-event","event_type":"biochemical_relationship","label":"Riboflavin-derived FAD, iron-sulfur centers and niacin-derived NAD work alongside molybdenum.","description":"The XDH form transfers purine-derived electrons through its iron-sulfur centers and FAD to NAD+, producing NADH.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"9fbf2e03-16a9-5ca7-965c-0bfc07ca24da","slug":"nadh","display_name":"NADH","entity_type_key":"small_molecule"},"role":"product","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"e2cd7179-f218-54e8-9ce9-7a836ae35fac","slug":"fad","display_name":"FAD","entity_type_key":"small_molecule"},"role":"electron transfer cofactor","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"02107865-f169-5624-9ea4-9448a4cce185","slug":"iron-sulfur-2fe2s","display_name":"[2Fe-2S] iron-sulfur cluster","entity_type_key":"chemical_species"},"role":"electron transfer cofactor","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"8de34d8a-46dc-512c-a82f-d169747b496e","slug":"xdh","display_name":"Human xanthine oxidoreductase / XDH","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"283ed24b-06a1-50aa-9281-df3bac6ce37e","slug":"nad-plus","display_name":"NAD+","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"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\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Recombinant human XDH variants with urate, superoxide and NO assays","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Xanthine, oxygen and inorganic nitrite assays","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Canonical electron-transfer mechanism stated in this primary article; not an experiment on dietary B2 or niacin depletion.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Molybdenum research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"molybdenum","display_name":"Molybdenum","entity_type_key":"nutrient_element"}},{"dimension":"organism","value_text":"Homo sapiens protein","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Riboflavin-derived FAD, iron-sulfur centers and niacin-derived NAD work alongside molybdenum.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[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","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified human enzyme","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"2d7b1df3-1e74-5540-8e48-bf683b5b6a38","evidence_kind":"source_excerpt","locator":"Lines 768-779","start_line":768,"end_line":779,"excerpt":"### mo-xdh-nad\nThe XDH form transfers purine-derived electrons through its iron-sulfur centers and FAD to NAD+, producing NADH.\nCondition category: normal\nnutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Riboflavin-derived FAD, iron-sulfur centers and niacin-derived NAD work alongside molybdenum.\norganism: Homo sapiens protein\ntissue_or_cell_type: Purified human enzyme\nexperimental_model: Recombinant human XDH variants with urate, superoxide and NO assays\nlimitations: Canonical electron-transfer mechanism stated in this primary article; not an experiment on dietary B2 or niacin depletion.\nexposure: Xanthine, oxygen and inorganic nitrite assays\nevidence_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\"}\n[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","model_system":"Recombinant human XDH variants with urate, superoxide and NO assays","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? 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