{"id":"86441ae0-b41d-501e-ac35-b1e623ecd4da","stable_key":"0ad8610d-d575-5870-b7cd-763a9f750783:copper-cox17-sco1-handoff","predicate":"transfers_copper_and_electrons_to","statement":"Cu(I)-COX17 with two disulfides transferred copper and two electrons to oxidized SCO1, producing copper-loaded SCO1 and apo-COX17 with three disulfides.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"091e0a38-d498-55aa-b58a-9efe6009502e","mechanism_event_label":"Copper delivery also changes the receiving protein into a form that can bind it.","subject":{"id":"07fe038d-b4c1-52b9-86af-b9199956bdd0","slug":"cox17-cu-i-two-disulfides","display_name":"Human Cu(I)-COX17 with two disulfides","entity_type_key":"protein_state"},"object":{"id":"afff9340-c805-5c05-9509-a7550d010ec0","slug":"sco1-oxidized","display_name":"Human SCO1 with oxidized copper-binding cysteines","entity_type_key":"protein_state"},"evidence_count":1,"mechanism_event":{"id":"091e0a38-d498-55aa-b58a-9efe6009502e","stable_key":"0ad8610d-d575-5870-b7cd-763a9f750783:copper-cox17-sco1-handoff-event","event_type":"biochemical_relationship","label":"Copper delivery also changes the receiving protein into a form that can bind it.","description":"Cu(I)-COX17 with two disulfides transferred copper and two electrons to oxidized SCO1, producing copper-loaded SCO1 and apo-COX17 with three disulfides.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"ec57ba8c-2035-54ce-bce7-023395121d31","slug":"cox17","display_name":"Human cytochrome c oxidase copper chaperone COX17","entity_type_key":"protein"},"role":"parent protein","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"6c18f07d-6a6e-5dcd-8294-2a3b3ee9c27c","slug":"sco1","display_name":"Human cytochrome c oxidase assembly protein SCO1","entity_type_key":"protein"},"role":"parent protein","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"5ed97fb4-0ce6-5f6f-96f9-429c9c69d95f","slug":"sco1-cu-i","display_name":"Human copper(I)-loaded SCO1","entity_type_key":"protein_state"},"role":"product","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"7b407296-6cec-58ff-b23e-32b325745125","slug":"cox17-apo-three-disulfides","display_name":"Human apo-COX17 with three disulfides","entity_type_key":"protein_state"},"role":"product","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"07fe038d-b4c1-52b9-86af-b9199956bdd0","slug":"cox17-cu-i-two-disulfides","display_name":"Human Cu(I)-COX17 with two disulfides","entity_type_key":"protein_state"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""},{"entity":{"id":"afff9340-c805-5c05-9509-a7550d010ec0","slug":"sco1-oxidized","display_name":"Human SCO1 with oxidized copper-binding cysteines","entity_type_key":"protein_state"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":5,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/copper-research/18458339.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"1e2740a864c2c21568eae7933027e4c9bb16b985478ebbf946d4d2067ba777f8\", \"start_char\": 0, \"end_char\": 1482, \"text_sha256\": \"1e2740a864c2c21568eae7933027e4c9bb16b985478ebbf946d4d2067ba777f8\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Purified-protein metal and electron transfer experiments","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Defined COX17 and SCO redox states; glutathione reduction","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Biochemical transfer mechanism; the same coupled reaction was not observed with SCO2. These results are not proof that glutathione supplementation repairs COX assembly.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Copper research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"copper","display_name":"Copper","entity_type_key":"nutrient_element"}},{"dimension":"organism","value_text":"Human proteins","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Copper delivery also changes the receiving protein into a form that can bind it.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[copper-p18458339] Mitochondrial copper(I) transfer from Cox17 to Sco1 is coupled to electron transfer. (2008). https://pubmed.ncbi.nlm.nih.gov/18458339/ DOI: 10.1073/pnas.0800019105","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Mitochondrial intermembrane-space protein system","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"d0a401b6-6673-509d-b296-70a5a35aca5d","evidence_kind":"source_excerpt","locator":"Lines 611-622","start_line":611,"end_line":622,"excerpt":"### copper-cox17-sco1-handoff\nCu(I)-COX17 with two disulfides transferred copper and two electrons to oxidized SCO1, producing copper-loaded SCO1 and apo-COX17 with three disulfides.\nCondition category: normal\nnutrient_topic: Copper research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Copper delivery also changes the receiving protein into a form that can bind it.\norganism: Human proteins\ntissue_or_cell_type: Mitochondrial intermembrane-space protein system\nexperimental_model: Purified-protein metal and electron transfer experiments\nlimitations: Biochemical transfer mechanism; the same coupled reaction was not observed with SCO2. These results are not proof that glutathione supplementation repairs COX assembly.\nexposure: Defined COX17 and SCO redox states; glutathione reduction\nevidence_span: {\"source_cache\": \"artifacts/copper-research/18458339.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"1e2740a864c2c21568eae7933027e4c9bb16b985478ebbf946d4d2067ba777f8\", \"start_char\": 0, \"end_char\": 1482, \"text_sha256\": \"1e2740a864c2c21568eae7933027e4c9bb16b985478ebbf946d4d2067ba777f8\"}\n[copper-p18458339] Mitochondrial copper(I) transfer from Cox17 to Sco1 is coupled to electron transfer. (2008). https://pubmed.ncbi.nlm.nih.gov/18458339/ DOI: 10.1073/pnas.0800019105","model_system":"Purified-protein metal and electron transfer experiments","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [copper-p18458339] Mitochondrial copper(I) transfer from Cox17 to Sco1 is coupled to electron transfer. (2008). https://pubmed.ncbi.nlm.nih.gov/18458339/ DOI: 10.1073/pnas.0800019105","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"9afba495-cbdc-51aa-998e-70a930dba3be","stable_key":"import-0ad8610d-d575-5870-b7cd-763a9f750783","title":"Copper: transport, cuproenzymes, deficiency, excess and nutrient interactions (2026-09-17)","document_type":"imported_text","citation_label":"AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text.","file_path":"","sha256":"84b0f62b2dae6835fa26902be87625c003c6c707492d3007e8f9d15420669008","revision_id":"d7e35b8b-3f77-56d9-90b5-5f542c63f321","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}