Catalytic site nucleotide and inorganic phosphate dependence of the conformation of the .epsilon. subunit in the Escherichia coli adenosinetriphosphatase-Reference-Cited by-同舟云学术

Catalytic site nucleotide and inorganic phosphate dependence of the conformation of the .epsilon. subunit in the Escherichia coli adenosinetriphosphatase

Published:1991-02-05 Issue:5 Volume:30 Page:1278-1284
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Mendel-Hartvig Janet,Capaldi Roderick A.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00219a017

Reference51 articles.

1. Thermodynamic analyses of the catalytic pathway of F1-ATPase from Escherichia coli. Implications regarding the nature of energy coupling by F1-ATPases.

2. A perspective of the binding change mechanism for ATP synthesis 1

3. Ligand-induced conformational changes in the Escherichia coli F1 adenosine triphosphatase probed by trypsin digestion

4. Adenosine Triphosphatase from Rat Liver Mitochondria

5. Energy-dependent Enhancement of Aurovertin Fluorescence

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