Abstract
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).
Copyright © 2012 Elsevier B.V. All rights reserved.
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*
Substances
-
Escherichia coli Proteins
-
Saccharomyces cerevisiae Proteins
-
Vacuolar Proton-Translocating ATPases
-
Proton-Translocating ATPases