Nature Structural & Molecular Biology11, 135 - 141 (2004)
Published online: 18 January 2004; | doi:10.1038/nsmb718
Proton-powered subunit rotation in single membrane-bound F0F1-ATP synthase
Manuel Diez1, Boris Zimmermann1, Michael Börsch2, Marcelle König3, Enno Schweinberger3, Stefan Steigmiller1, Rolf Reuter1, Suren Felekyan3, Volodymyr Kudryavtsev3, Claus A M Seidel3
& Peter Gräber1
1
Institut für Physikalische Chemie, Albert-Ludwigs-Universität Freiburg, Albertstrasse 23 a, 79104 Freiburg, Germany.
Synthesis of ATP from ADP and phosphate, catalyzed by F0F1-ATP synthases, is the most abundant physiological reaction in almost any cell. F0F1-ATP synthases are membrane-bound enzymes that use the energy derived from an electrochemical proton gradient for ATP formation. We incorporated double-labeled F0F1-ATP synthases from Escherichia coli into liposomes and measured single-molecule fluorescence resonance energy transfer (FRET) during ATP synthesis and hydrolysis. The 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.
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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.
