Stochastic Four-State Mechanochemical Model of F1-ATPase |
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| Authors: | WU Wei-Xia ZHAN Yong ZHAO Tong-Jun HAN Ying-Rong CHEN Ya-Fei |
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| Affiliation: | 1.Institute of Biophysics, School of Science, Hebei University of Technology, Tianjin 300130, China;2.Science Education Department, Beijing Institute of Graphic Communication, Beijing 102600, China |
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| Abstract: | ![]()
F1-ATPase, a part of ATP synthase, can synthesize and hydrolyze ATP moleculars in which the central γ-subunit rotates inside the α3β3 cylinder. Astochastic four-state mechanochemical coupling model of F$_{1}$-ATPase isstudied with the aid of the master equation. In this model, the ATPhydrolysis and synthesis are dependent on ATP, ADP, and Pi concentrations.The effects of ATP concentration, ADP concentration, and the external torqueon the occupation probability of binding-state, the rotation rate and thediffusion coefficient of F1-ATPase are investigated. Moreover, theresults from this model are compared with experiments. The mechanochemicalmechanism F1-ATPase is qualitatively explained by the model. |
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| Keywords: | F1-ATPase four-state mechanochemical model hydrolysis reaction the master equation |
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