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

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

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1
Department of Biochemistry, Iwate Medical University, Yahaba, Iwate, Japan. futaim@iwate-med.ac.jp

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).

PMID:
22459334
DOI:
10.1016/j.bbabio.2012.03.015
[Indexed for MEDLINE]
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