2012 Fiscal Year Final Research Report
Effect of fluctuation and hydration on the function of F1-ATPase motor
| Project Area | Water plays a key role in ATP hydrolysis and ATP-driven functions of proteins |
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| Project/Area Number |
20118010
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| Research Category |
Grant-in-Aid for Scientific Research on Innovative Areas (Research in a proposed research area)
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| Allocation Type | Single-year Grants |
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| Review Section |
Complex systems
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| Research Institution | Chuo University |
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Principal Investigator |
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| Project Period (FY) |
2008 – 2012
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| Keywords | ATP / 水和 / 分子モーター / F1-ATPase / 非平衡 |
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| Research Abstract |
F1-ATPase is a rotary molecular motor which couples the hydrolysis/synthesis of ATP molecule with the rotation of internal γsubunit. We imposed an opposing external torque to find stall torque under various conditions. From the stall torque, we demonstrated that the F1-ATPase converts the free energy of ATP hydrolysis to the kinetic energy of the rotation at nearly 100 % efficiency. At far from equilibrium, by measuring the nonequilibrium fluctuation, we demonstrated that the F1-ATPase dissipates the free energy of ATP hydrolysis in the rotational degree of freedom at nearly 100 % efficiency. Furthermore, we found that these remarkable properties were well explained by the shape of driving potential and the timing of its switching.
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Research Products
(10 results)
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[Journal Article] Temperature Dependence of the Rotation and Hydrolysis Activities of F_1-ATPase2008
Author(s)
Furuike, S., Adachi, K., Sakaki, N., Shimo-Kon, R., Itoh, H., Muneyuki, E., Yoshida, M., Kinosita, K
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Journal Title
Biophys. J
Volume: 95
Pages: 761-770
Peer Reviewed
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