ABSTRACT
ATP synthase, also called F1Fo-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 (ECF1Fo). 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.
© 2000 by Company of Biologists
2000
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