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Article

Identification of the betaTP site in the x-ray structure of F1-ATPase as the high-affinity catalytic site.

Proceedings of the National Academy of Sciences of the United States of America - 20 Nov 2007

Mao Hui Z, Weber Joachim

Abstract excerpt

ATP synthase uses a unique rotary mechanism to couple ATP synthesis and hydrolysis to transmembrane proton translocation. The F(1) subcomplex has three catalytic nucleotide binding sites, one on each beta subunit, with widely differing affinities for MgATP or MgADP. During rotational catalysis, the sites switch their affinities. The affinity of each site is determined by the position of the central gamma subunit....

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Identifiers

PMID: 18003896
DOI: 10.1073/pnas.0709322104
PMCID: PMC2141802

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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