Summary
F1-ATPase is a molecular motor in which the central γ subunit rotates inside the cylinder made of α3β3 subunits. The rotation is powered by ATP hydrolysis in three catalytic sites, and reverse rotation of the γ subunit by an external force leads to ATP synthesis in the catalytic sites. Single-molecule studies have revealed how the mechanical rotation is coupled to the chemical reactions in the three catalytic sites: binding/release of ATP, ADP, and phosphate, and hydrolysis/synthesis of ATP.
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Acknowledgements
We thank the members of Kinosita and Yoshida labs for collaboration and discussion, R. Kanda-Terada for technical support, K. Sakamaki, M. Fukatsu, and H. Umezawa for encouragement and lab management. This work was supported by Grants-in-Aids for Specially Promoted Research from the Ministry of Education, Sports, Culture, Science and Technology, Japan.
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Adachi, K. et al. (2010). Chemo-Mechanical Coupling in the Rotary Molecular Motor F1-ATPase. In: Gräslund, A., Rigler, R., Widengren, J. (eds) Single Molecule Spectroscopy in Chemistry, Physics and Biology. Springer Series in Chemical Physics, vol 96. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-02597-6_14
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