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Journal of Experimental Biology, Vol 203, Issue 1 29-33, Copyright © 2000 by Company of Biologists

JOURNAL ARTICLES

Cross-linking and electron microscopy studies of the structure and functioning of the Escherichia coli ATP synthase

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.




© The Company of Biologists Ltd 2000