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Fate of nucleotides bound to reconstituted Fo-F1 during adenosine 5'-triphosphate synthesis activation or hydrolysis: role of protein inhibitor and hysteretic inhibition.
Penin F, Di Pietro A, Godinot C, Gautheron DC. Penin F, et al. Among authors: godinot c. Biochemistry. 1988 Dec 13;27(25):8969-74. doi: 10.1021/bi00425a014. Biochemistry. 1988. PMID: 2906804
The protein ATPase inhibitor entraps about five nucleotides in pig heart mitochondrial F1, one at least being a triphosphate [Di Pietro, A., Penin, F., Julliard, J.H., Godinot, C., & Gautheron, D.C. (1988) Biochem. Biophys. Res. Commun. 152, 1319-1325]. T …
The protein ATPase inhibitor entraps about five nucleotides in pig heart mitochondrial F1, one at least being a triphosphate [Di Pietro, A., …
Inhibition of mitochondrial F1-ATPase activity by an anti-alpha subunit monoclonal antibody which modifies interactions between catalytic and regulatory sites.
Moradi-Améli M, Julliard JH, Godinot C. Moradi-Améli M, et al. Among authors: godinot c. J Biol Chem. 1989 Jan 25;264(3):1361-7. J Biol Chem. 1989. PMID: 2536364 Free article.
This phase has been correlated to the binding of 5'-p-fluorosulfonylbenzoyladenosine to regulatory sites (Di Pietro, A., Godinot, C., Martin, J. C., and Gautheron, D. C. (1979) Biochemistry 18, 1738-1745). The inhibition of ATP hydrolysis is concomitan …
This phase has been correlated to the binding of 5'-p-fluorosulfonylbenzoyladenosine to regulatory sites (Di Pietro, A., Godinot, …
130 results