Proton-powered subunit rotation in single membrane-bound F0F1-ATP synthase.

Abstract:

:Synthesis of ATP from ADP and phosphate, catalyzed by F(0)F(1)-ATP synthases, is the most abundant physiological reaction in almost any cell. F(0)F(1)-ATP synthases are membrane-bound enzymes that use the energy derived from an electrochemical proton gradient for ATP formation. We incorporated double-labeled F(0)F(1)-ATP synthases from Escherichia coli into liposomes and measured single-molecule fluorescence resonance energy transfer (FRET) during ATP synthesis and hydrolysis. The gamma subunit rotates stepwise during proton transport-powered ATP synthesis, showing three distinct distances to the b subunits in repeating sequences. The average durations of these steps correspond to catalytic turnover times upon ATP synthesis as well as ATP hydrolysis. The direction of rotation during ATP synthesis is opposite to that of ATP hydrolysis.

journal_name

Nat Struct Mol Biol

authors

Diez M,Zimmermann B,Börsch M,König M,Schweinberger E,Steigmiller S,Reuter R,Felekyan S,Kudryavtsev V,Seidel CA,Gräber P

doi

10.1038/nsmb718

keywords:

subject

Has Abstract

pub_date

2004-02-01 00:00:00

pages

135-41

issue

2

eissn

1545-9993

issn

1545-9985

pii

nsmb718

journal_volume

11

pub_type

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