F1-ATPase rotates by an asymmetric, sequential mechanism using all three catalytic subunits
Author:
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Structural Biology
Link
http://www.nature.com/articles/nsmb1296.pdf
Reference42 articles.
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2. Kinosita, K., Jr., Adachi, K. & Itoh, H. Rotation of F1-ATPase: how an ATP-driven molecular machine may work. Annu. Rev. Biophys. Biomol. Struct. 33, 245–268 (2004).
3. Kayalar, C., Rosing, J. & Boyer, P.D. An alternating site sequence for oxidative phosphorylation suggested by measurement of substrate binding patterns and exchange reaction inhibitions. J. Biol. Chem. 252, 2486–2491 (1977).
4. Gresser, M.J., Myers, J.A. & Boyer, P.D. Catalytic site cooperativity of beef heart mitochondrial F1 adenosine triphosphatase. Correlations of initial velocity, bound intermediate, and oxygen exchange measurements with an alternating three-site model. J. Biol. Chem. 257, 12030–12038 (1982).
5. Grubmeyer, C., Cross, R.L. & Penefsky, H.S. Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate constants for elementary steps in catalysis at a single site. J. Biol. Chem. 257, 12092–12100 (1982).
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