Synthase (H+ ATPase): Coupling between catalysis, mechanical work, and proton translocation

Masamitsu Futai; Hiroshi Omote; Yoshihiro Sambongi; Yoh Wada

doi:10.1016/S0005-2728(00)00080-3

Synthase (H⁺ ATPase): Coupling between catalysis, mechanical work, and proton translocation

Masamitsu Futai, Hiroshi Omote, Yoshihiro Sambongi, Yoh Wada

Research output: Contribution to journal › Review article › peer-review

42 Citations (Scopus)

Abstract

Coupling with electrochemical proton gradient, ATP synthase (F₀F₁) synthesizes ATP from ADP and phosphate. Mutational studies on high-resolution structure have been useful in understanding this complicated membrane enzyme. We discuss mainly the mechanism of catalysis in the β subunit of F₁ sector and roles of the γ subunit in energy coupling. The γ-subunit rotation during catalysis is also discussed. Copyright (C) 2000 Elsevier Science B.V.

Original language	English
Pages (from-to)	276-288
Number of pages	13
Journal	Biochimica et Biophysica Acta - Bioenergetics
Volume	1458
Issue number	2-3
DOIs	https://doi.org/10.1016/S0005-2728(00)00080-3
Publication status	Published - May 31 2000
Externally published	Yes

Keywords

ATP synthesis
Catalytic site
FF
H ATPase
Proton transport
Rotational catalysis

ASJC Scopus subject areas

Biophysics
Biochemistry
Cell Biology

Access to Document

10.1016/S0005-2728(00)00080-3

Cite this

@article{1437916aa81348379c8b691e70088031,

title = "Synthase (H+ ATPase): Coupling between catalysis, mechanical work, and proton translocation",

abstract = "Coupling with electrochemical proton gradient, ATP synthase (F0F1) synthesizes ATP from ADP and phosphate. Mutational studies on high-resolution structure have been useful in understanding this complicated membrane enzyme. We discuss mainly the mechanism of catalysis in the β subunit of F1 sector and roles of the γ subunit in energy coupling. The γ-subunit rotation during catalysis is also discussed. Copyright (C) 2000 Elsevier Science B.V.",

keywords = "ATP synthesis, Catalytic site, FF, H ATPase, Proton transport, Rotational catalysis",

author = "Masamitsu Futai and Hiroshi Omote and Yoshihiro Sambongi and Yoh Wada",

note = "Funding Information: Studies of our laboratory cited in this article are supported by Japanese Ministry of Education, Science and Culture and Japan Science and Technology Corporation. We are grateful to Dr. Ashley Spies for the critical reading of the manuscript.",

year = "2000",

month = may,

day = "31",

doi = "10.1016/S0005-2728(00)00080-3",

language = "English",

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pages = "276--288",

journal = "Biochimica et Biophysica Acta - Bioenergetics",

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TY - JOUR

T1 - Synthase (H+ ATPase)

T2 - Coupling between catalysis, mechanical work, and proton translocation

AU - Futai, Masamitsu

AU - Omote, Hiroshi

AU - Sambongi, Yoshihiro

AU - Wada, Yoh

N1 - Funding Information: Studies of our laboratory cited in this article are supported by Japanese Ministry of Education, Science and Culture and Japan Science and Technology Corporation. We are grateful to Dr. Ashley Spies for the critical reading of the manuscript.

PY - 2000/5/31

Y1 - 2000/5/31

N2 - Coupling with electrochemical proton gradient, ATP synthase (F0F1) synthesizes ATP from ADP and phosphate. Mutational studies on high-resolution structure have been useful in understanding this complicated membrane enzyme. We discuss mainly the mechanism of catalysis in the β subunit of F1 sector and roles of the γ subunit in energy coupling. The γ-subunit rotation during catalysis is also discussed. Copyright (C) 2000 Elsevier Science B.V.

AB - Coupling with electrochemical proton gradient, ATP synthase (F0F1) synthesizes ATP from ADP and phosphate. Mutational studies on high-resolution structure have been useful in understanding this complicated membrane enzyme. We discuss mainly the mechanism of catalysis in the β subunit of F1 sector and roles of the γ subunit in energy coupling. The γ-subunit rotation during catalysis is also discussed. Copyright (C) 2000 Elsevier Science B.V.

KW - ATP synthesis

KW - Catalytic site

KW - FF

KW - H ATPase

KW - Proton transport

KW - Rotational catalysis

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U2 - 10.1016/S0005-2728(00)00080-3

DO - 10.1016/S0005-2728(00)00080-3

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AN - SCOPUS:0034738058

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JO - Biochimica et Biophysica Acta - Bioenergetics

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