scholarly journals Cross-linking and labeling of the Escherichia coli F1F0-ATP synthase reveal a compact hydrophilic portion of F0 close to an F1 catalytic subunit.

1983 ◽  
Vol 258 (23) ◽  
pp. 14599-14609 ◽  
Author(s):  
J P Aris ◽  
R D Simoni
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Catalytic Subunit ◽  
Cross Linking ◽  
F1f0 Atp Synthase

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

2000 ◽  
Vol 203 (1) ◽  
pp. 29-33 ◽  
Author(s):  
R.A. Capaldi ◽  
B. Schulenberg ◽  
J. Murray ◽  
R. Aggeler
Keyword(s):  
Electron Microscopy ◽  
Escherichia Coli ◽  
Oxidative Phosphorylation ◽  
Atp Synthase ◽  
Proton Gradient ◽  
Cross Linking ◽  
Combination Of Methods ◽  
Chemical Cross Linking

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.

Sign in / Sign up

Export Citation Format

Share Document