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

Masamitsu Futai, Hiroshi Omote, Yoshihiro Sambongi, Yoh Wada

Research output: Contribution to journalArticle

37 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 languageEnglish
Pages (from-to)276-288
Number of pages13
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1458
Issue number2-3
DOIs
Publication statusPublished - May 31 2000
Externally publishedYes

Fingerprint

Proton-Translocating ATPases
Catalysis
Protons
Adenosine Triphosphate
Adenosine Diphosphate
Phosphates
Membranes
Enzymes

Keywords

  • ATP synthesis
  • Catalytic site
  • FF
  • H ATPase
  • Proton transport
  • Rotational catalysis

ASJC Scopus subject areas

  • Biophysics

Cite this

Synthase (H+ ATPase) : Coupling between catalysis, mechanical work, and proton translocation. / Futai, Masamitsu; Omote, Hiroshi; Sambongi, Yoshihiro; Wada, Yoh.

In: Biochimica et Biophysica Acta - Bioenergetics, Vol. 1458, No. 2-3, 31.05.2000, p. 276-288.

Research output: Contribution to journalArticle

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