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Article

The nucleotide binding affinities of two critical conformations of Escherichia coli ATP synthase.

Archives of biochemistry and biophysics - 15 Aug 2021

Li Yunxiang, Valdez Neydy A, Mnatsakanyan Nelli, Weber Joachim

Abstract excerpt

ATP synthase is essential in aerobic energy metabolism, and the rotary catalytic mechanism is one of the core concepts to understand the energetic functions of ATP synthase. Disulfide bonds formed by oxidizing a pair of cysteine mutations halted the rotation of the γ subunit in two critical conformations, the ATP-waiting dwell (αE284C/γQ274C) and the catalytic dwell (αE284C/γL276C). Tryptophan fluorescence was...

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PMID: 33991499
DOI: 10.1016/j.abb.2021.108899
PMCID: PMC8278868

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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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