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• W2963487095 abstract "Our understanding of the rotary-coupling mechanism of F1-ATPase has been greatly enhanced in the last decade by advances in X-ray crystallography, single-molecular imaging, and theoretical models. Recently, Volkán-Kacsó and Marcus [S. Volkán-Kacsó, R. A. Marcus, Proc. Natl. Acad. Sci. U.S.A. 112, 14230 (2015)] presented an insightful thermodynamic model based on the Marcus reaction theory coupled with an elastic structural deformation term to explain the observed γ-rotation angle dependence of the adenosine triphosphate (ATP)/adenosine diphosphate (ADP) exchange rates of F1-ATPase. Although the model is successful in correlating single-molecule data, it is not in agreement with the available theoretical results. We describe a revision of the model, which leads to consistency with the simulation results and other experimental data on the F1-ATPase rotor compliance. Although the free energy liberated on ATP hydrolysis by F1-ATPase is rapidly dissipated as heat and so cannot contribute directly to the rotation, we show how, nevertheless, F1-ATPase functions near the maximum possible efficiency. This surprising result is a consequence of the differential binding of ATP and its hydrolysis products ADP and Pi along a well-defined pathway." @default.
• W2963487095 created "2019-07-30" @default.
• W2963487095 creator A5022993160 @default.
• W2963487095 creator A5076499540 @default.
• W2963487095 date "2019-07-24" @default.
• W2963487095 modified "2023-10-18" @default.
• W2963487095 title "Insights into the origin of the high energy-conversion efficiency of F ₁ -ATPase" @default.
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• W2963487095 doi "https://doi.org/10.1073/pnas.1906816116" @default.
• W2963487095 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6690014" @default.
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