The coupled chemomechanics of the F(1)-ATPase molecular motor.
The enzyme F(1)-ATPase is a rotary nanomotor in which the central gamma subunit rotates inside the cavity made of alpha(3)beta(3) subunits. The experiments showed that the rotation proceeds in steps of 120 degrees and each 120 degrees step consists of 80 degrees and 40 degrees substeps. Here the Author proposes a stochastic wave mechanics of the F(1)-ATPase motor and combines it with the structure-based kinetics of the F(1)-ATPase to form a chemomechanic coupled model. The model can reproduce quantitatively and explain the experimental observations about the F(1) motor. Using the model, several rate-limited situations about gamma subunit rotation are proposed, the effects of the friction and the load on the substeps are investigated and the chemomechanic coupled time during ATP hydrolysis cycle is determined.
Xu
Lizhong
L
Yanshan University, Qinhuangdao, 066004, China. xlz@ysu.edu.cn
D000255:Adenosine Triphosphate / Q000737:chemistry; D007700:Kinetics; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000502:physiology*; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000502:physiology*
D020409:Molecular Motor Proteins; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases