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(2019). https://pubmed.ncbi.nlm.nih.gov/31167903/ DOI: 10.1042/bcj20190143","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified human sulfite oxidase","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"56738d51-37b8-596b-a780-385e2e0afe17","evidence_kind":"source_excerpt","locator":"Lines 1093-1104","start_line":1093,"end_line":1104,"excerpt":"### mo-suox-nitrite\nHuman SUOX reduced nitrite to NO at the molybdenum center, with steady-state turnover supported in a sulfite/cytochrome-c system.\nCondition category: normal\nnutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: SUOX can perform additional redox chemistry under the tested conditions.\norganism: Homo sapiens protein\ntissue_or_cell_type: Purified human sulfite oxidase\nexperimental_model: Human SUOX kinetics, spectroscopy and electron-transfer variants\nlimitations: Biochemical capacity; contribution to human physiology requires separate evidence.\nexposure: Nitrite with sulfite and cytochrome c\nevidence_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\"}\n[mo-p31167903] Mechanism of nitrite-dependent NO synthesis by human sulfite oxidase. 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