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  • Title: Rotational catalysis in proton pumping ATPases: from E. coli F-ATPase to mammalian V-ATPase.
    Author: Futai M, Nakanishi-Matsui M, Okamoto H, Sekiya M, Nakamoto RK.
    Journal: Biochim Biophys Acta; 2012 Oct; 1817(10):1711-21. PubMed ID: 22459334.
    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).
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