【摘 要】
：
V1-ATPase is a rotary molecular motor in which the mechanical rotation of the rotor DF subunits against the stator A3B3 ring is driven by the chemical energy of ATP hydrolysis.Recently, we verified th
【机 构】
：
Department of Applied Chemistry, The University of Tokyo, Bunkyo-ku, Japan
【出 处】
：
The 9th Asian Biophysics Association Symposium (ABA2015)(第九届
论文部分内容阅读
V1-ATPase is a rotary molecular motor in which the mechanical rotation of the rotor DF subunits against the stator A3B3 ring is driven by the chemical energy of ATP hydrolysis.Recently, we verified the rotation of E.hirae V1-ATPase (EhV1) by single-molecule analysis.EhV1 unidirectionally rotated in the counterclockwise direction, exhibiting three pausing positions separated by 120°.In these pauses, the elementary reaction steps of the ATP hydrolysis, such as ATP binding, ATP cleavage, ADP and Pi releases, occur at three catalytic sites (A subunits) of the stator A3B3 ring.However, it is difficult for wildtype EhV1 to distinguish which elementary reaction steps of each A subunits occur at each pausing positions, because the rates of the elementary reaction steps for three A subunits are identical.
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