Regulation of cytochrome c oxidase by interaction of ATP at two binding sites, one on subunit VIa.

doi:10.1021/bi00205a020

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Article

Regulation of cytochrome c oxidase by interaction of ATP at two binding sites, one on subunit VIa.

Biochemistry - 4 Oct 1994

Taanman J W, Turina P, Capaldi R A

Abstract excerpt

Cytochrome c oxidase isolated from a wild-type yeast strain and a mutant in which the gene for subunit VIa had been disrupted were used to study the interaction of adenine nucleotides with the enzyme complex. At low ionic strength (25 mM potassium phosphate), in the absence of nucleotides, the cy...

Topics

Adenosine Diphosphate
Adenosine Triphosphate
Affinity Labels
Amino Acid Sequence
Animals
Azides
Cattle
Electron Transport
Electron Transport Complex IV
Isoenzymes
Kidney
Models, Chemical
Molecular Sequence Data
Mutation
Myocardium
Protein Conformation
Saccharomyces cerevisiae
Species Specificity

Source

Open in PubMed

Identifiers

PMID: 7918401
DOI: 10.1021/bi00205a020

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7918401-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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