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Автор Kinosita, Kazuhiko
Автор Adachi, Kengo
Автор Itoh, Hiroyasu
Дата выпуска 2004
dc.description ▪ 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, Fo, 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 is free energy obtained by ATP hydrolysis converted to the mechanical work of rotation, and how is mechanical work done on F1 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.
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Издатель Annual Reviews
Копирайт Annual Reviews
Название ROTATION OF F1-ATPASE: How an ATP-Driven Molecular Machine May Work
DOI 10.1146/annurev.biophys.33.110502.132716
Print ISSN 1056-8700
Журнал Annual Review of Biophysics and Biomolecular Structure
Том 33
Первая страница 245
Последняя страница 268
Аффилиация Kinosita, Kazuhiko; Center for Integrative Bioscience, Okazaki National Research Institutes, Higashiyama 5-1, Myodaiji, Okazaki 444-8585, Japan; email: kazuhiko@ims.ac.jp ; adachi@ims.ac.jp

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