Molecular mechanisms of rotational catalysis in the F0F1 ATP synthase

Robert K. Nakamoto, Christian J. Ketchum, Phillip H. Kuo, Yelena B. Peskova, Marwan K. Al-Shawi

Research output: Contribution to journalReview articlepeer-review

35 Scopus citations

Abstract

Rotation of the F0F1 ATP synthase γ subunit drives each of the three catalytic sites through their reaction pathways. The enzyme completes three cycles and synthesizes or hydrolyzes three ATP for each 360°rotation of the γ subunit. Mutagenesis studies have yielded considerable information on the roles of interactions between the rotor γ subunit and the catalytic β subunits. Amino acid substitutions, such as replacement of the conserved γMet-23 by Lys, cause altered interactions between γ and β subunits that have dramatic effects on the transition state of the steady state ATP synthesis and hydrolysis reactions. The mutations also perturb transmission of specific conformational information between subunits which is important for efficient conversion of energy between rotation and catalysis, and render the coupling between catalysis and transport inefficient. Amino acid replacements in the transport domain also affect the steady state catalytic transition state indicating that rotation is involved in coupling to transport.

Original languageEnglish (US)
Pages (from-to)289-299
Number of pages11
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1458
Issue number2-3
DOIs
StatePublished - May 31 2000

Keywords

  • Adenosine triphosphate synthase
  • Coupling
  • FF
  • Mutational analysis
  • Subunit interaction
  • Transition state thermodynamics

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

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