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F1-ATPase changes its conformations upon phosphate release.
Masaike T, Muneyuki E, Noji H, Kinosita K Jr, Yoshida M. Masaike T, et al. Among authors: yoshida m. J Biol Chem. 2002 Jun 14;277(24):21643-9. doi: 10.1074/jbc.M110297200. Epub 2002 Mar 5. J Biol Chem. 2002. PMID: 11880367 Free article.
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.
The epsilon subunit in F0F1-ATPase/synthase undergoes drastic conformational rearrangement, which involves the transition of two C-terminal helices between a hairpin "down"-state and an extended "up"-state, and the enzyme with the up-fixed epsilon cannot catalyze ATP hydrolysis b …
The epsilon subunit in F0F1-ATPase/synthase undergoes drastic conformational rearrangement, which involves the transition of two C-terminal …
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.
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