Rotational catalysis in proton pumping ATPases: from E. coli F-ATPase to mammalian V-ATPase

Biochim Biophys Acta. 2012 Oct;1817(10):1711-21. doi: 10.1016/j.bbabio.2012.03.015. Epub 2012 Mar 20.


We focus on the rotational catalysis of Escherichia coli F-ATPase (ATP synthase, F(O)F(1)). Using a probe with low viscous drag, we found stochastic fluctuation of the rotation rates, a flat energy pathway, and contribution of an inhibited state to the overall behavior of the enzyme. Mutational analyses revealed the importance of the interactions among β and γ subunits and the β subunit catalytic domain. We also discuss the V-ATPase, which has different physiological roles from the F-ATPase, but is structurally and mechanistically similar. We review the rotation, diversity of subunits, and the regulatory mechanism of reversible subunit dissociation/assembly of Saccharomyces cerevisiae and mammalian complexes. This article is part of a Special Issue entitled: 17th European Bioenergetics Conference (EBEC 2012).

Publication types

  • Review

MeSH terms

  • Animals
  • Catalytic Domain
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism*
  • Humans
  • Protein Structure, Tertiary
  • Proton-Translocating ATPases / chemistry
  • Proton-Translocating ATPases / genetics
  • Proton-Translocating ATPases / metabolism*
  • Saccharomyces cerevisiae / enzymology
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism
  • Vacuolar Proton-Translocating ATPases / chemistry
  • Vacuolar Proton-Translocating ATPases / genetics
  • Vacuolar Proton-Translocating ATPases / metabolism*


  • Escherichia coli Proteins
  • Saccharomyces cerevisiae Proteins
  • Vacuolar Proton-Translocating ATPases
  • Proton-Translocating ATPases