cytochrome bd-I ubiquinol oxidase complex
Cytochrome bd-I ubiquinol oxidase complex is a membrane-bound CydAB respiratory terminal oxidase with small bd-I accessory subunits that oxidizes ubiquinol, reduces molecular oxygen to water, and contributes to the respiratory proton motive force. [DOI:10.1126/science.aay0967]
Synonyms: cytochrome bd-I oxidase
Components
| Component | Type | Part of / acts on | Grounding | Genes | Stoichiometry | Essential | Role |
|---|---|---|---|---|---|---|---|
| cytochrome bd-I ubiquinol oxidase subunit I | Protein | part of | InterPro:IPR002585 | cydA | ESSENTIAL | Large membrane subunit of the cytochrome bd-I terminal oxidase core that houses heme cofactors used for ubiquinol-to-oxygen electron flow.
| |
| cytochrome bd-I ubiquinol oxidase subunit II | Protein | part of | InterPro:IPR003317 | cydB | ESSENTIAL | Second large membrane subunit of the CydAB cytochrome bd-I oxidase core.
| |
| cytochrome bd-I ubiquinol oxidase CydX small subunit | Protein | part of | InterPro:IPR011724 | cydX, ybgT | UNKNOWN | Small single-pass membrane subunit resolved in the E. coli bd-I oxidase.
| |
| YnhF-like cytochrome bd-I small subunit | Protein | part of | InterPro:IPR047743 | ynhF | UNKNOWN | YnhF-like single-pass membrane subunit resolved with the E. coli bd-I oxidase and associated with a CydH NCBIfam model.
|
Canonical examples
NCBITaxon:562Escherichia coli — Bacterial species used for the four-subunit cytochrome bd-I oxidase structure deposited as PDB:6RKO. [PDB:6RKO]
Functions
- ubiquinol:oxygen terminal oxidase activity — Cytochrome bd-I oxidizes ubiquinol, reduces molecular oxygen to water, and conserves respiratory-chain energy through a bd-type architecture distinct from heme-copper cytochrome c oxidases.
InterPro:IPR002585InterPro describes CydA-family proteins as alternative oxidases that oxidize ubiquinol and reduce oxygen as part of the electron transport chain.DOI:10.1126/science.aay0967Safarian et al. 2019 solved the E. coli cytochrome bd-I oxidase structure deposited as PDB:6RKO.PMID:31604309The PubMed abstract for Safarian et al. 2019 describes cytochrome bd-type quinol oxidases as respiratory-chain enzymes that catalyze molecular-oxygen reduction to water and are structurally unrelated to mitochondrial cytochrome c oxidases.
Mechanism graphs
Cytochrome bd-I reduces oxygen with ubiquinol electrons (FUNCTION)
Cytochrome bd-I oxidase converts ubiquinol and oxygen to ubiquinone and water through its CydA and CydB large subunits and contributes to respiratory energy conservation.
| Subject | Predicate | Object | Evidence |
|---|---|---|---|
| cytochrome bd-I ubiquinol oxidase complex | enables | ubiquinol:oxygen terminal oxidase activity |
|
| cytochrome bd-I ubiquinol oxidase subunit I | contributes to | ubiquinol:oxygen terminal oxidase activity |
|
| cytochrome bd-I ubiquinol oxidase subunit II | contributes to | ubiquinol:oxygen terminal oxidase activity |
|
| ubiquinol | donates electrons to | ubiquinol:oxygen terminal oxidase activity |
|
| molecular oxygen | accepts electrons in | ubiquinol:oxygen terminal oxidase activity |
|
| ubiquinol:oxygen terminal oxidase activity | produces | ubiquinone |
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| ubiquinol:oxygen terminal oxidase activity | produces | water |
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| ubiquinol:oxygen terminal oxidase activity | contributes to | transmembrane proton motive force |
|
Discussions
- CURATION_TODO (OPEN): Resolve how CydX/YbgT and YnhF-like small subunits should be split across cytochrome bd-I, bd-II, and two-subunit CydAB oxidases. PDB:6RKO supports a four-subunit E. coli bd-I oxidase with CydX and YnhF, while PDB:7NKZ supports a two-subunit Mycobacterium tuberculosis bd oxidase; this record should not project E. coli bd-I small subunits onto every bd-type oxidase.
Evidence
GO:0098803Gene Ontology cellular-component term for respiratory-chain protein complexes.GO:0070069Gene Ontology cellular-component term for cytochrome complexes.GO:0016682Gene Ontology molecular-function term for oxidoreductase activity with a diphenol-related donor and oxygen as acceptor; no exact cytochrome bd ubiquinol oxidase activity term was found.InterPro:IPR002585InterPro family for cytochrome ubiquinol oxidase subunit 1.InterPro:IPR003317InterPro family for cytochrome ubiquinol oxidase subunit 2.InterPro:IPR011724InterPro family for the CydX/YbgT small subunit.InterPro:IPR047743InterPro family for the YnhF-like CydH small subunit.DOI:10.1126/science.aay0967Safarian et al. 2019, Active site rearrangement and structural divergence in prokaryotic respiratory oxidases, Science.PMID:31604309PubMed identifier for Safarian et al. 2019 as reported by the RCSB PDB:6RKO primary citation.PDB:6RKORCSB Protein Data Bank entry for the E. coli cytochrome bd-I oxidase structure from Safarian et al. 2019.
Curation history
2026-09-24T06:59:35Zcodex · CREATED_RECORD — Scaffolded by scripts/new_record.py2026-09-24T07:00:39Zcodex · EXPANDED_RECORD — Added respiratory-chain and cytochrome-complex parentage, PDB:6RKO E. coli cytochrome bd-I oxidase components with InterPro CydA, CydB, CydX, and YnhF-like family groundings, UniProtKB-backed gene aliases, terminal ubiquinol:oxygen oxidase function, literature/PDB evidence, a compact bd-I function graph, and a small-subunit scope TODO.2026-09-24T07:02:54Zcodex · REFINED_GRAPH — Replaced the orphan CydAB graph node with direct CydA and CydB contribution edges and grounded water production in PMID:31604309.2026-09-24T07:13:46Zcodex · ADDRESSED_REVIEW — Addressed review issues #1462, #1463, and #1464 by adding a ubiquinone product node and edge, narrowing the YnhF/CydH role wording, and tying the heme-copper divergence claim to PMID:31604309.
Source: data/structures/energy_complex/cytochrome_bd_i_ubiquinol_oxidase_complex.yaml