respiratory chain complex IV
Respiratory chain complex IV is a membrane-bound cytochrome c oxidase complex that transfers electrons from reduced cytochrome c to dioxygen and couples oxygen reduction to proton translocation across a respiratory membrane. [GO:0045277]
Synonyms: cytochrome c oxidase complex; electron transport complex IV
Components
| Component | Type | Part of / acts on | Grounding | Genes | Stoichiometry | Essential | Role |
|---|---|---|---|---|---|---|---|
| bacterial cytochrome c oxidase subunit I | Protein | part of | InterPro:IPR014241 | ctaD, ctaDII, coxA, caaA | ESSENTIAL | Catalytic core subunit that binds the heme-copper binuclear center where dioxygen is reduced.
| |
| cytochrome c oxidase subunit II | Protein | part of | Reviewed label only (reviewed name; no accession asserted) | ctaC, ctaB, coiI, coxB | ESSENTIAL | CuA-bearing subunit on the cytochrome-c acceptor side of the terminal oxidase.
| |
| cytochrome c oxidase subunit III | Protein | part of | Reviewed label only (reviewed name; no accession asserted) | ctaE, coiII, coxC | UNKNOWN | Membrane core subunit of the aa3 cytochrome c oxidase complex.
| |
| bacterial aa3-type cytochrome c oxidase subunit IV | Protein | part of | InterPro:IPR012422 | ctaH | UNKNOWN | Small single-pass membrane subunit present in bacterial aa3 cytochrome c oxidases such as the Paracoccus complex.
|
Canonical examples
NCBITaxon:266Paracoccus denitrificans — Bacterial source of the four-subunit aa3 cytochrome c oxidase structure deposited as PDB:1QLE. [PDB:1QLE]
Functions
- cytochrome-c oxidase activity
GO:0004129— Complex IV oxidizes reduced cytochrome c, reduces molecular oxygen to water, and moves protons across the respiratory membrane.GO:0004129GO:0004129 defines the cytochrome-c oxidase reaction as cytochrome c oxidation and oxygen reduction coupled to proton translocation.DOI:10.1074/jbc.274.47.33296Harrenga and Michel 1999 solved the four-subunit Paracoccus denitrificans cytochrome c oxidase structure deposited as PDB:1QLE.
Mechanism graphs
Complex IV reduces oxygen with cytochrome c electrons (FUNCTION)
Respiratory complex IV oxidizes reduced cytochrome c, reduces oxygen to water, and contributes to a proton motive force across the respiratory membrane.
| Subject | Predicate | Object | Evidence |
|---|---|---|---|
| respiratory chain complex IV | enables | cytochrome-c oxidase activity |
|
| reduced cytochrome c | donates electrons to | cytochrome-c oxidase activity |
|
| bacterial cytochrome c oxidase subunit I | contributes to | cytochrome-c oxidase activity |
|
| cytochrome c oxidase subunit II | contributes to | cytochrome-c oxidase activity |
|
| molecular oxygen | accepts electrons in | cytochrome-c oxidase activity |
|
| cytochrome-c oxidase activity | produces | water |
|
| cytochrome-c oxidase activity | contributes to | transmembrane proton motive force |
|
Discussions
- CURATION_TODO (OPEN): Resolve exact source-neutral families for cytochrome c oxidase subunits II and III, and add lineage-specific mitochondrial, cbb3, ba3, and caa3 accessory subunits without collapsing them into the Paracoccus aa3 four-subunit model. GO exactly grounds respiratory chain complex IV across mitochondrial and bacterial cytochrome c oxidases, but the first component model is anchored to the PDB:1QLE Paracoccus aa3 complex and should not invent exact family CURIEs for subunits whose InterPro entries are broad or domain-only.
Evidence
GO:0045277Gene Ontology cellular-component term for respiratory chain complex IV.GO:0098803Gene Ontology cellular-component term for respiratory-chain protein complexes.GO:0004129Gene Ontology molecular-function term for cytochrome-c oxidase activity.InterPro:IPR014241InterPro family for bacterial cytochrome c oxidase subunit I.InterPro:IPR045187InterPro family for cytochrome c/quinol oxidase subunit II.InterPro:IPR014222InterPro domain entry for cytochrome c oxidase subunit II.InterPro:IPR024791InterPro family for cytochrome c oxidase subunit III.InterPro:IPR012422InterPro entry for bacterial aa3-type cytochrome c oxidase subunit IV.DOI:10.1074/jbc.274.47.33296Harrenga and Michel 1999, The Cytochrome C Oxidase from Paracoccus Denitrificans Does not Change the Metal Center Ligation Upon Reduction, Journal of Biological Chemistry.PMID:10559205PubMed identifier for Harrenga and Michel 1999 as reported by the RCSB PDB:1QLE primary citation.PDB:1QLERCSB Protein Data Bank entry for the Paracoccus denitrificans four-subunit cytochrome c oxidase structure from Harrenga and Michel 1999.
Curation history
2026-09-24T06:25:40Zcodex · CREATED_RECORD — Scaffolded by scripts/new_record.py2026-09-24T06:26:59Zcodex · EXPANDED_RECORD — Added GO respiratory-chain parentage and synonymy, PDB:1QLE Paracoccus denitrificans cytochrome c oxidase components, InterPro-grounded subunit I and IV entries, reviewed-label-only subunit II and III entries, cytochrome-c oxidase activity, literature/PDB evidence, a compact complex IV function graph, and a component-grounding TODO.2026-09-24T06:27:58Zcodex · REVISED_COMPONENTS — Added Paracoccus denitrificans cytochrome c oxidase gene-symbol aliases ctaDII, ctaB, coiI, and coiII verified against the PDB:1QLE UniProtKB component accessions.2026-09-24T06:39:50Zcodex · ADDRESS_REVIEW — #1459/#1460: qualified the InterPro-grounded subunit I component as bacterial and replaced broad subunit-II graph evidence with the cytochrome-c-specific InterPro subunit-II domain entry.
Source: data/structures/energy_complex/respiratory_chain_complex_iv.yaml