Cytochrome c oxidase from eucaryotes but not from procaryotes is allosterically inhibited by ATP.

doi:10.1002/iub.7510450522

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Article

Cytochrome c oxidase from eucaryotes but not from procaryotes is allosterically inhibited by ATP.

Biochemistry and molecular biology international - 1 Aug 1998

Follmann K, Arnold S, Ferguson-Miller S, Kadenbach B

Abstract excerpt

The activity of reconstituted cytochrome c oxidase from bovine heart but not from Rhodobacter sphaeroides is allosterically inhibited by intraliposomal ATP, which binds to subunit IV. The activity of cytochrome c oxidase of wild-type yeast and of a subunit VIa-deleted yeast mutant, measured with...

Topics

Adenosine Diphosphate
Adenosine Triphosphate
Allosteric Regulation
Animals
Binding Sites
Cattle
Electron Transport Complex IV
Kinetics
Mitochondria
Mitochondria, Heart
Mutation
Rhodobacter sphaeroides
Saccharomyces cerevisiae

Source

Open in PubMed

Identifiers

PMID: 9739469
DOI: 10.1002/iub.7510450522

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9739469-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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