Stochastic Four-State Mechanochemical Model of F1-ATPase

F1-ATPase, a part of ATP synthase, can synthesize and hydrolyze ATP moleculars in which the central γ-subunit rotates inside the α3β3 cylinder. A stochastic four-state mechanochemical coupling model of F1-ATPase is studied with the aid of the master equation. In this model, the ATP hydrolysis and sy...

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Bibliographic Details
Published inCommunications in theoretical physics Vol. 54; no. 10; pp. 630 - 634
Main Author 吴魏霞 展永 赵同军 韩英荣 陈娅斐
Format Journal Article
LanguageEnglish
Published IOP Publishing 15.10.2010
Subjects
ATP分子
ATP酶
三磷酸腺苷酶
力模型
旋转速度
机械力
浓度依赖性
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ISSN0253-6102
DOI10.1088/0253-6102/54/4/09

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Summary:F1-ATPase, a part of ATP synthase, can synthesize and hydrolyze ATP moleculars in which the central γ-subunit rotates inside the α3β3 cylinder. A stochastic four-state mechanochemical coupling model of F1-ATPase is studied with the aid of the master equation. In this model, the ATP hydrolysis and synthesis are dependent on ATP, ADP, and Pi concentrations. The effects of ATP concentration, ADP concentration, and the external torque on the occupation probability of binding-state, the rotation rate and the diffusion coefficient of F1-ATPase are investigated. Moreover, the results from this model are compared with experiments. The mechanochemical mechanism F1-ATPase is qualitatively explained by the model.
Bibliography:S511.01
11-2592/O3
TS941.562
F1-ATPase, four-state mechanochemical model, hydrolysis reaction, the master equation
ISSN:0253-6102
DOI:10.1088/0253-6102/54/4/09