We summarize our current view of the reaction mechanism in F1-ATPase as it has emerged from experiment, theory, and computational studies over the last several years. ATP catalysis in the catalytic binding pockets of F1 takes place without the release of any significant free energy and is efficiently driven by the combined action of two water molecules utilizing a so-called protein-relay mechanism. The chemical reaction itself is controlled by the spatial position of a key arginine residue.
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Abrahams, J., Leslie, A., Lutter, R., and Walker, J. (1994). Nature 370, 621–628.
Ahmad, Z., and Senior, A. E. (2004). J. Biol. Chem. 44, 46057–46064.
Berg, J. M., Tymoczko, J. L., and Stryer, L. (2002). Biochemistry, 5th edn., W. H. Freeman, New York.
Böckmann, R. A., and Grubmüller, H. (2002). Nature Struct. Biol. 9, 198–202.
Dittrich, M., Hayashi, S., and Schulten, K. (2003). Biophys. J. 85, 2253–2266.
Dittrich, M., Hayashi, S., and Schulten, K. (2004). Biophys. J. 87, 2954–2967.
Li, G., and Cui, Q. (2004). J. Phys. Chem. B 108, 3342–3357.
Nishizaka, T., Oiwa, K., Noji, H., Kimura, S., Muneyuki, E., Yoshida, M., and Kinosita, K., Jr. (2004). Nat. Struct. Mol. Biol. 11, 142–148.
Oster, G., and Wang, H. (2000). Biochim. Biophys. Acta 1458, 482–510.
Scheidig, A. J., Burmester, C., and Goody, R. S. (1999). Structure 7, 1311–1324.
Shimabukuro, K., Yasuda, R., Muneyuki, E., Hara, K. Y., Kinosita, K., Jr., and Yoshida, M. (2003). Proc. Natl. Acad. Sci. U.S.A. 100, 14731–14736.
Strajbl, M., Shurki, A., and Warshel, A. (2003). Proc. Natl. Acad. Sci. U.S.A. 100, 14834–14839.
Weber, J., Nadanaciva, S., and Senior, A. E. (2000). FEBS Lett. 483, 1–5.
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Dittrich, M., Schulten, K. Zooming in on ATP Hydrolysis in F1 . J Bioenerg Biomembr 37, 441–444 (2005). https://doi.org/10.1007/s10863-005-9487-7
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DOI: https://doi.org/10.1007/s10863-005-9487-7