F_1-ATPase, a part of ATP synthase, can synthesize and hydrolyze ATP moleculars in which the centralγ-subunit rotates inside the α_3β_3 cylinder.A stochastic four-state mechanochemical coupling model of F_1-ATPase ...F_1-ATPase, a part of ATP synthase, can synthesize and hydrolyze ATP moleculars in which the centralγ-subunit rotates inside the α_3β_3 cylinder.A stochastic four-state mechanochemical coupling model of F_1-ATPase isstudied 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 theoccupation probability of binding-state, the rotation rate and the diffusion coefficient of F_1-ATPase are investigated.Moreover, the results from this model are compared with experiments.The mechanochemical mechanism F_1-ATPase isqualitatively explained by the model.展开更多
基金Supported by the National Natural Science Foundation of China under Grant No.10847118the National Natural Science Foundation of the City of Tianjin under Grant No.08JCYBJC00900 the Science Research Program of Education office of Hebei Province under Grant No.2008427
文摘F_1-ATPase, a part of ATP synthase, can synthesize and hydrolyze ATP moleculars in which the centralγ-subunit rotates inside the α_3β_3 cylinder.A stochastic four-state mechanochemical coupling model of F_1-ATPase isstudied 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 theoccupation probability of binding-state, the rotation rate and the diffusion coefficient of F_1-ATPase are investigated.Moreover, the results from this model are compared with experiments.The mechanochemical mechanism F_1-ATPase isqualitatively explained by the model.
