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

Authors
Futai, M Omote, H Sambongi, Y Wada, Y
Citation
M. Futai et al., Synthase (H+ ATPase): coupling between catalysis, mechanical work, and proton translocation, BBA-BIOENER, 1458(2-3), 2000, pp. 276-288
Citations number
73
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
ISSN journal
00052728 → ACNP
Volume
1458
Issue
2-3
Year of publication
2000
Pages
276 - 288
Database
ISI
SICI code
0005-2728(20000531)1458:2-3<276:S(ACBC>2.0.ZU;2-6
Abstract
Coupling with electrochemical proton gradient, ATP synthase (F0F1) synthesi zes ATP from ADP and phosphate. Mutational studies on high-resolution struc ture have been useful in understanding this complicated membrane enzyme. We discuss mainly the mechanism of catalysis in the beta subunit of F-1 secto r and roles of the gamma subunit in energy coupling. The gamma-subunit rota tion during catalysis is also discussed. (C) 2000 Elsevier Science B.V. All rights reserved.