Coupling of Rotation and Catalysis in F1-ATPase Revealed by Single-Molecule Imaging and Manipulation-Reference-Cited by-同舟云学术

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Coupling of Rotation and Catalysis in F1-ATPase Revealed by Single-Molecule Imaging and Manipulation

Published:2007-07 Issue:2 Volume:130 Page:309-321
ISSN:0092-8674
Container-title:Cell
language:en
Short-container-title:Cell

Author:

Adachi Kengo,Oiwa Kazuhiro,Nishizaka Takayuki,Furuike Shou,Noji Hiroyuki,Itoh Hiroyasu,Yoshida Masasuke,Kinosita Kazuhiko

Publisher

Elsevier BV

Subject

General Biochemistry, Genetics and Molecular Biology

Reference31 articles.

1. Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria;Abrahams;Nature,1994

2. Stepping rotation of F1-ATPase visualized through angle-resolved single-fluorophore imaging;Adachi;Proc. Natl. Acad. Sci. USA,2000

3. The Escherichia coli FOF1 γM23K uncoupling mutant has a higher K0.5 for Pi. Transition state analysis of this mutant and others reveals that synthesis and hydrolysis utilize the same kinetic pathway;Al-Shawi;Biochemistry,1997

4. The binding change mechanism for ATP synthase - some probabilities and possibilities;Boyer;Biochim. Biophys. Acta,1993

5. The present status of the binding-change mechanism and its relation to ATP formation by chloroplasts;Boyer,1981

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