ATP synthase: What we know about ATP hydrolysis and what we do not know about ATP synthesis

Joachim Weber, Alan E. Senior

Research output: Contribution to journalReview article

133 Scopus citations

Abstract

In ATP synthase, X-ray structures, demonstration of ATP-driven γ-subunit rotation, and tryptophan fluorescence techniques to determine catalytic site occupancy and nucleotide binding affinities have resulted in pronounced progress in understanding ATP hydrolysis, for which a mechanism is presented here. In contrast, ATP synthesis remains enigmatic. The molecular mechanism by which ADP is bound in presence of a high ATP/ADP concentration ratio is a fundamental unknown; similarly P(i) binding is not understood. Techniques to measure catalytic site occupancy and ligand binding affinity changes during net ATP synthesis are much needed. Relation of these parameters to γ-rotation is a further goal. A speculative model for ATP synthesis is offered. Copyright (C) 2000 Elsevier Science B.V.

Original languageEnglish
Pages (from-to)300-309
Number of pages10
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1458
Issue number2-3
DOIs
StatePublished - May 31 2000

Keywords

  • ATP synthase
  • Oxidative phosphorylation
  • Proton pumping

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