The Catalytic Mechanism Based on a Four-state Model of F1-ATPase

摘要：

F1-ATPase, a rotary motor enzyme, can catalyse ATP hydrolysis in which the central γ-subunit ratates inside the α3β3 cylinder. Here, a four-state catalytic model of F1-ATPase is studied in which we think that the ATP hydrolysis and synthesis are ATP-dependent and ADP/Pi-dependent, respectively. The results show that the catalytic ratation mechanism of F1-ATPase is affected distinctly by the ATP/ADP/Pi concentrations. The model accords well with the expermental observations. Moreover, when the external load exists, the mean rotation rate of F1-ATPase is also affected apparently, and the external torque which decreases the mean ratation rate of the F1 motor to zero equals to the constant one which is produced during the ratation of the motor.

作者: Wu Weixia Zhan Yong Chen Yafei Han Yingrong

作者单位: Science Education Department Beijing Institute of Graphic Communication Beijing, China Institute of Institute of Biophysics, School of Science Hebei University of Technology Tianjin, China

会议类型: 国际会议

会议名称: The 4th International Conference on Bioinformatics and Biomedical Engineering(第四届IEEE生物信息与生物医学工程国际会议 iCBBE 2010)

会议地点: 成都

会议语种:英文

页码: 1-4

在线出版日期: 2010-06-18（万方平台首次上网日期，不代表论文的发表时间）