Cross-linking and electron microscopy studies of the structure and functioning of the Escherichia coli ATP synthase.
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.
Capaldi
R A
RA
Institute of Molecular Biology, University of Oregon, Eugene, OR 97403-1229, USA. rcapaldi@oregon.uoregon.edu
Schulenberg
B
B
Murray
J
J
Aggeler
R
R
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003432:Cross-Linking Reagents; D004926:Escherichia coli / Q000201:enzymology*; D008854:Microscopy, Electron; D008958:Models, Molecular; D015394:Molecular Structure; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure
D003432:Cross-Linking Reagents; D006180:Proton-Translocating ATPases