scholarly journals Subunit rotation in Escherichia coli FoF1-ATP synthase during oxidative phosphorylation

1997 ◽  
Vol 94 (20) ◽  
pp. 10583-10587 ◽  
Author(s):  
Y. Zhou ◽  
T. M. Duncan ◽  
R. L. Cross
Keyword(s):  
Escherichia Coli ◽  
Oxidative Phosphorylation ◽  
Atp Synthase ◽  
Subunit Rotation ◽  
Fof1 Atp Synthase

scholarly journals Spotlighting motors and controls of single FoF1-ATP synthase

2013 ◽  
Vol 41 (5) ◽  
pp. 1219-1226 ◽  
Author(s):  
Michael Börsch ◽  
Thomas M. Duncan
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Single Molecule ◽  
Conformational Changes ◽  
Structural Information ◽  
E Coli ◽  
Single Molecule Fret ◽  
Membrane Enzyme ◽  
Subunit Rotation ◽  
Fof1 Atp Synthase

Subunit rotation is the mechanochemical intermediate for the catalytic activity of the membrane enzyme FoF1-ATP synthase. smFRET (single-molecule FRET) studies have provided insights into the step sizes of the F1 and Fo motors, internal transient elastic energy storage and controls of the motors. To develop and interpret smFRET experiments, atomic structural information is required. The recent F1 structure of the Escherichia coli enzyme with the ϵ-subunit in an inhibitory conformation initiated a study for real-time monitoring of the conformational changes of ϵ. The present mini-review summarizes smFRET rotation experiments and previews new smFRET data on the conformational changes of the CTD (C-terminal domain) of ϵ in the E. coli enzyme.

scholarly journals The Regulatory C-Terminal Domain of Subunit   of FoF1 ATP Synthase Is Dispensable for Growth and Survival of Escherichia coli

2011 ◽  
Vol 193 (8) ◽  
pp. 2046-2052 ◽  
Author(s):  
N. Taniguchi ◽  
T. Suzuki ◽  
M. Berney ◽  
M. Yoshida ◽  
G. M. Cook
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Growth And Survival ◽  
Terminal Domain ◽  
Fof1 Atp Synthase

scholarly journals An alternative role of FoF1-ATP synthase in Escherichia coli: synthesis of thiamine triphosphate

2013 ◽  
Vol 3 (1) ◽  
Author(s):  
Tiziana Gigliobianco ◽  
Marjorie Gangolf ◽  
Bernard Lakaye ◽  
Bastien Pirson ◽  
Christoph von Ballmoos ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Thiamine Triphosphate ◽  
Fof1 Atp Synthase

scholarly journals Direct observation of steps in c-ring rotation of Escherichia coli FOF1-ATP synthase

2010 ◽  
Vol 1797 ◽  
pp. 34 ◽  
Author(s):  
Ryota Iino ◽  
Khek-Chian Tham ◽  
Kazuhito V. Tabata ◽  
Hiroshi Ueno ◽  
Hiroyuki Noji
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Direct Observation ◽  
Ring Rotation ◽  
Fof1 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.

scholarly journals The regulatory subunit ε in Escherichia coli FOF1-ATP synthase

2018 ◽  
Vol 1859 (9) ◽  
pp. 775-788 ◽  
Author(s):  
Hendrik Sielaff ◽  
Thomas M. Duncan ◽  
Michael Börsch
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Regulatory Subunit ◽  
Fof1 Atp Synthase
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