期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 108, 期 44, 页码 17951-17956出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1106787108
关键词
electrorotation; molecular motor; nonequilibrium physics
资金
- Japan Science and Technology Agency (J.S.T.)
- [18074001]
- [17049015]
- [19037022]
- [18031033]
- [21023007]
- [20118010]
- [21740291]
- Grants-in-Aid for Scientific Research [23654137] Funding Source: KAKEN
F-1-ATPase is a nanosized biological energy transducer working as part of FoF1-ATP synthase. Its rotary machinery transduces energy between chemical free energy and mechanical work and plays a central role in the cellular energy transduction by synthesizing most ATP in virtually all organisms. However, information about its energetics is limited compared to that of the reaction scheme. Actually, fundamental questions such as how efficiently F-1-ATPase transduces free energy remain unanswered. Here, we demonstrated reversible rotations of isolated F-1-ATPase in discrete 120 degrees steps by precisely controlling both the external torque and the chemical potential of ATP hydrolysis as a model system of FoF1-ATP synthase. We found that the maximum work performed by F-1-ATPase per 120 degrees step is nearly equal to the thermodynamical maximum work that can be extracted from a single ATP hydrolysis under a broad range of conditions. Our results suggested a 100% free-energy transduction efficiency and a tight mechanochemical coupling of F-1-ATPase.
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