Component
Human cytochrome c oxidase copper chaperone COX17
Human cytochrome c oxidase copper chaperone COX17. Species, exposure and limitations are retained in each linked claim.
1 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
How nutrients influence it
Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
How nutrients reach it in more than one step
Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.
Tracing routes…
What it does
Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.
Where it participates (unsigned role)
Cu(I)-COX17 with two disulfides transferred copper and two electrons to oxidized SCO1, producing copper-loaded SCO1 and apo-COX17 with three disulfides.
Experimental context and source evidence
- evidence_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"}
- experimental_model
- Purified-protein metal and electron transfer experiments
- exposure
- Defined COX17 and SCO redox states; glutathione reduction
- limitations
- Biochemical transfer mechanism; the same coupled reaction was not observed with SCO2. These results are not proof that glutathione supplementation repairs COX assembly.
- nutrient_topic
- Copper research collection; topical membership is not evidence of a direct dietary effect. · Copper
- organism
- Human proteins
- plain_language
- Copper delivery also changes the receiving protein into a form that can bind it.
- primary_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
- tissue_or_cell_type
- Mitochondrial intermembrane-space protein system
Copper: transport, cuproenzymes, deficiency, excess and nutrient interactions (2026-09-17) · lines 611–622
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified-protein metal and electron transfer experiments · source_derived_draft · unverified_draft
### copper-cox17-sco1-handoff Cu(I)-COX17 with two disulfides transferred copper and two electrons to oxidized SCO1, producing copper-loaded SCO1 and apo-COX17 with three disulfides. Condition category: normal nutrient_topic: Copper research collection; topical membership is not evidence of a direct dietary effect. plain_language: Copper delivery also changes the receiving protein into a form that can bind it. organism: Human proteins tissue_or_cell_type: Mitochondrial intermembrane-space protein system experimental_model: Purified-protein metal and electron transfer experiments limitations: Biochemical transfer mechanism; the same coupled reaction was not observed with SCO2. These results are not proof that glutathione supplementation repairs COX assembly. exposure: Defined COX17 and SCO redox states; glutathione reduction evidence_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"} [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
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.