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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| Published in | Communications in theoretical physics Vol. 54; no. 10; pp. 630 - 634 |
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| Main Author | |
| Format | Journal Article |
| Language | English |
| Published |
IOP Publishing
15.10.2010
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| Subjects | |
| Online Access | Get full text |
| ISSN | 0253-6102 |
| DOI | 10.1088/0253-6102/54/4/09 |
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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. 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. |
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| AbstractList | 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. |
| Author | 吴魏霞 展永 赵同军 韩英荣 陈娅斐 |
| AuthorAffiliation | Institute of Biophysics, School of Science, Hebei University of Technology, Tianjin 300130, China Science Education Department, Beijing Institute of Graphic Communication, Beijing 102600, China |
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| Notes | S511.01 11-2592/O3 TS941.562 F1-ATPase, four-state mechanochemical model, hydrolysis reaction, the master equation |
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| Snippet | 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... |
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| StartPage | 630 |
| SubjectTerms | 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 |
| Title | Stochastic Four-State Mechanochemical Model of F1-ATPase |
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