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Journal of Experimental Biology, Vol 203, Issue 1 29-33, Copyright © 2000 by Company of Biologists
JOURNAL ARTICLES |
RA Capaldi, B Schulenberg, J Murray and R Aggeler
Institute of Molecular Biology, University of Oregon, Eugene, OR 97403-1229, USA. rcapaldi@oregon.uoregon.edu
ATP synthase, also called F(1)F(o)-ATPase, catalyzes the synthesis of ATP during oxidative phosphorylation. The enzyme is reversible and is able to use ATP to drive a proton gradient for transport purposes. Our work has focused on the enzyme from Escherichia coli (ECF(1)F(o)). We have used a combination of methods to study this enzyme, including electron microscopy and chemical cross-linking. The utility of these two approaches in particular, and the important insights they give into the structure and mechanism of the ATP synthase, are reviewed.
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S. Kawasaki-Nishi, T. Nishi, and M. Forgac Yeast V-ATPase Complexes Containing Different Isoforms of the 100-kDa a-subunit Differ in Coupling Efficiency and in Vivo Dissociation J. Biol. Chem., May 18, 2001; 276(21): 17941 - 17948. [Abstract] [Full Text] [PDF]
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O. Y. Dmitriev and R. H. Fillingame Structure of Ala20right-arrow Pro/Pro64right-arrow Ala Substituted Subunit c of Escherichia coli ATP Synthase in Which the Essential Proline Is Switched between Transmembrane Helices J. Biol. Chem., July 13, 2001; 276(29): 27449 - 27454. [Abstract] [Full Text] [PDF]
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