Abstract
Annual Review of Biophysics and Biomolecular Structure
(doi:10.1146/annurev.biophys.33.110502.132716)
First posted online on January 16, 2004Rotation of F1-ATPase: How an ATP-Driven Molecular Machine May WorkKazuhiko Kinosita, Jr.Center for Integrative Bioscience, Okazaki National Research Institutes, Okazaki 444-8585, Japan kazuhiko@ims.ac.jp Kengo AdachiCenter for Integrative Bioscience, Okazaki National Research Institutes, Okazaki 444-8585, Japan adachi@ims.ac.jp Hiroyasu ItohTsukuba Research Laboratory, Hamatsu Photonics KK, and CREST "Creation and Application of Soft Nano-Machine, the Hyperfunctional Molecular Machine" Team 13, Tsukuba 300-2635, Japan hiritoh@hpk.trc-net.co.jp
 Abstract F1-ATPase is a rotary motor made of a single protein molecule. Its rotation is driven by free energy obtained by ATP hydrolysis. In vivo, another motor F0 presumably rotates the F1 motor in the reverse direction, reversing also the chemical reaction in F1 to let it synthesize ATP. Here we attempt to answer two related questions: how free energy obtained by ATP hydrolysis is converted to the mechanical work of rotation, and how mechanical work done on F1 is converted to free energy to produce ATP. After summarizing single-molecule observations of F1 rotation, we introduce a toy model and discuss its free-energy diagrams, to possibly answer the above questions. We also discuss the efficiency of molecular motors in general.
Expected online publication date for the Annual Review of Biophysics and Biomolecular Structure Volume 33 is May 5, 2004. Please see http://www.annualreviews.org/catalog/pub_dates.asp for revised estimates.
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