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F0F1-ATPase/synthase is geared to the synthesis mode by conformational rearrangement of epsilon subunit in response to proton motive force and ADP/ATP balance.
Suzuki T, Murakami T, Iino R, Suzuki J, Ono S, Shirakihara Y, Yoshida M. Suzuki T, et al. Among authors: yoshida m. J Biol Chem. 2003 Nov 21;278(47):46840-6. doi: 10.1074/jbc.M307165200. Epub 2003 Jul 24. J Biol Chem. 2003. PMID: 12881515 Free article.
P., Rodgers, A. J. W., Aggeler, R., Wilce, M. C. J., Yoshida, M., and Capaldi, R. A. (2001) Proc. Natl. Acad. Sci. U. S. A. 98, 6560-6564). ...
P., Rodgers, A. J. W., Aggeler, R., Wilce, M. C. J., Yoshida, M., and Capaldi, R. A. (2001) Proc. Natl. Acad. Sci. U. S …
ATP-driven stepwise rotation of FoF1-ATP synthase.
Ueno H, Suzuki T, Kinosita K Jr, Yoshida M. Ueno H, et al. Among authors: yoshida m. Proc Natl Acad Sci U S A. 2005 Feb 1;102(5):1333-8. doi: 10.1073/pnas.0407857102. Epub 2005 Jan 24. Proc Natl Acad Sci U S A. 2005. PMID: 15668386 Free PMC article.
Probing conformations of the beta subunit of F0F1-ATP synthase in catalysis.
Masaike T, Suzuki T, Tsunoda SP, Konno H, Yoshida M. Masaike T, et al. Among authors: yoshida m. Biochem Biophys Res Commun. 2006 Apr 14;342(3):800-7. doi: 10.1016/j.bbrc.2006.02.017. Epub 2006 Feb 17. Biochem Biophys Res Commun. 2006. PMID: 16517239
A subcomplex of F0F1-ATP synthase (F0F1), alpha3beta3gamma, was shown to undergo the conformation(s) during ATP hydrolysis in which two of the three beta subunits have the "Closed" conformation simultaneously (CC conformation) [S.P. Tsunoda, E. Muneyuki, T. Amano, M. Yo …
A subcomplex of F0F1-ATP synthase (F0F1), alpha3beta3gamma, was shown to undergo the conformation(s) during ATP hydrolysis in which two of t …
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