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Article

Evidence of a subunit 4 (subunit b) dimer in favor of the proximity of ATP synthase complexes in yeast inner mitochondrial membrane.

Biochimica et biophysica acta - 11 Nov 1998

Spannagel C, Vaillier J, Arselin G, Graves P V, Grandier-Vazeille X, Velours J

Abstract excerpt

Yeast mitochondria having either the D54C or E55C mutations in subunit 4 (subunit b), which is a component of the ATP synthase stator, displayed a spontaneous disulfide bridge between two subunits 4. This dimer was not soluble upon Triton X-100 extraction either at concentrations which extract th...

Topics

Intracellular Membranes
Mitochondria
Mutation
Oligomycins
Proton-Translocating ATPases
Saccharomyces cerevisiae

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 9804970
DOI: 10.1016/s0005-2736(98)00174-6

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9804970-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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Evidence of a subunit 4 (subunit b) dimer in favor of the proximity of ATP synthase complexes in yeast inner mitochondrial membrane.PMID 9804970Read ↗

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