Mutational Analysis of ATP Synthase An Approach to Catalysis and Energy Coupling
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Springer US
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http://link.springer.com/content/pdf/10.1007/978-1-4615-4843-0_17
Reference113 articles.
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2. Abrahams, J. P., Leslie, A. G. W., Lutter, R., and Walker, J. E., 1994, Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria, Nature 370:621–628.
3. Aggeler, R., Haughton, M. A., and Capaldi, R. A., 1995, Disulfide bond formation between the COOH-terminal domain of the β subunits and the γ and ε subunits of the Escherichia coli F1 -ATPase: Structural implication and functional consequences, J. Biol. Chem. 270:9185–9191.
4. Aggeler, R., Cai, S. X., Keana, J. F. W., Koike, T., and Capaldi, R. A., 1993, The γ-subunit of the Escherichia coli F1-ATPase can be cross-linked near the glycine-rich loop region of a β-subunit when ADP+Mg2+ occupies catalytic sites but not when ATP+Mg2+ is bound, J. Biol. Chem. 268:20831–20837.
5. Allison, W S., Jault, J.-M., Zhuo, S., and Paik, S. R., 1992, Functional sites in F1-ATPases: Location and interactions, J. Bioenerg. Biomembr. 24:469–477.
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1. Synthase (H+ ATPase): coupling between catalysis, mechanical work, and proton translocation;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2000-05
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