Acceleration of the ATP-binding rate of F1-ATPase by forcible forward rotation |
| |
Authors: | Yuko Iko |
| |
Institution: | Institute of Scientific and Industrial Science, Osaka University, Mihogaoka 8-1, Ibaraki, Osaka 567-0047, Japan |
| |
Abstract: | F1-ATPase (F1) is a reversible ATP-driven rotary motor protein. When its rotary shaft is reversely rotated, F1 produces ATP against the chemical potential of ATP hydrolysis, suggesting that F1 modulates the rate constants and equilibriums of catalytic reaction steps depending on the rotary angle of the shaft. Although the chemomechanical coupling scheme of F1 has been determined, it is unclear how individual catalytic reaction steps depend on its rotary angle. Here, we report direct evidence that the ATP-binding rate of F1 increases upon the forward rotation of the rotor, and its binding affinity to ATP is enhanced by rotation. |
| |
Keywords: | F1 F1-ATPase Pi inorganic phosphate SEM scanning electron microscope |
本文献已被 ScienceDirect 等数据库收录! |
|