PMID:14730350

Citation	Diez, M, Zimmermann, B, Börsch, M, König, M, Schweinberger, E, Steigmiller, S, Reuter, R, Felekyan, S, Kudryavtsev, V, Seidel, CA and Gräber, P (2004) Proton-powered subunit rotation in single membrane-bound F0F1-ATP synthase. Nat. Struct. Mol. Biol. 11:135-41
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.
Links	PubMed Online version:10.1038/nsmb718
Keywords	Adenosine Triphosphate/metabolism; Adenylyl Imidodiphosphate/metabolism; Catalysis; Energy Transfer; Fluorescence; Hydrolysis; Proton-Translocating ATPases/metabolism; Protons
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.