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Article

Thermodynamic analyses of the catalytic pathway of F1-ATPase from Escherichia coli. Implications regarding the nature of energy coupling by F1-ATPases.

The Journal of biological chemistry - 15 Mar 1990

al-Shawi M K, Parsonage D, Senior A E

Abstract excerpt

Thermodynamic properties of 12 different F1-ATPase enzymes were analyzed in order to gain insights into the catalytic mechanism and the nature of energy coupling to delta mu H+. The enzymes were normal soluble Escherichia coli F1, a group of nine beta-subunit mutant soluble E. coli F1 enzymes (G1...

Topics

Adenosine Diphosphate
Adenosine Triphosphate
Catalysis
Escherichia coli
Hydrolysis
Kinetics
Mitochondria, Heart
Mutation
Phosphates
Protein Conformation
Proton-Translocating ATPases
Temperature

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Thermodynamics

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PMID: 2137823

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-2137823-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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