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

doi:10.1016/j.abb.2021.108899

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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...

Topics

Escherichia coli
Adenosine Triphosphate
Protein Binding
Protein Conformation
Oxidation-Reduction
Adenosine Diphosphate
Escherichia coli Proteins
Models, Molecular
Nucleotides
Mutation
Catalytic Domain

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Identifiers

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

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