Rotational catalysis in proton pumping ATPases: From E. coli F-ATPase to mammalian V-ATPase
Rotational catalysis in proton pumping ATPases: From E. coli F-ATPase to mammalian V-ATPase
We focus on the rotational catalysis of Escherichia coli F-ATPase (ATP synthase, FOF1). 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 ? and ? subunits and the ? 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
1711-1721
Futai, Masamitsu
c5675800-b53e-4302-ab49-51b70232b008
Nakanishi-Matsui, Mayumi
ae829e11-8227-442e-ad61-e6a5c37d15f4
Okamoto, Haruko
cea35380-7618-44c8-a268-47b0198cc7f9
Sekiya, Mizuki
9703d2e8-d17a-485e-8e95-86e4f22cc99a
Nakamoto, Robert K.
dba825bb-e171-4e00-93cd-b4b473db1c27
2012
Futai, Masamitsu
c5675800-b53e-4302-ab49-51b70232b008
Nakanishi-Matsui, Mayumi
ae829e11-8227-442e-ad61-e6a5c37d15f4
Okamoto, Haruko
cea35380-7618-44c8-a268-47b0198cc7f9
Sekiya, Mizuki
9703d2e8-d17a-485e-8e95-86e4f22cc99a
Nakamoto, Robert K.
dba825bb-e171-4e00-93cd-b4b473db1c27
Futai, Masamitsu, Nakanishi-Matsui, Mayumi, Okamoto, Haruko, Sekiya, Mizuki and Nakamoto, Robert K.
(2012)
Rotational catalysis in proton pumping ATPases: From E. coli F-ATPase to mammalian V-ATPase.
[in special issue: 17th European Bioenergetics Conference]
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1817 (10), .
(doi:10.1016/j.bbabio.2012.03.015).
(PMID:22459334)
Abstract
We focus on the rotational catalysis of Escherichia coli F-ATPase (ATP synthase, FOF1). 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 ? and ? subunits and the ? 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
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Published date: 2012
Organisations:
Centre for Biological Sciences
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Local EPrints ID: 362186
URI: http://eprints.soton.ac.uk/id/eprint/362186
ISSN: 0005-2728
PURE UUID: 4b2d7322-ad3f-4347-aba5-63f50f12361a
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Date deposited: 14 Mar 2014 14:17
Last modified: 14 Mar 2024 16:01
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Author:
Masamitsu Futai
Author:
Mayumi Nakanishi-Matsui
Author:
Haruko Okamoto
Author:
Mizuki Sekiya
Author:
Robert K. Nakamoto
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