Tight ATP and ADP binding in the noncatalytic sites ofEscherichia coliF1-ATPase is not affected by mutation of bulky residues in the ‘glycine-rich loop’-Reference-Cited by-同舟云学术

Tight ATP and ADP binding in the noncatalytic sites ofEscherichia coliF1-ATPase is not affected by mutation of bulky residues in the ‘glycine-rich loop’

Published:1990-10-29 Issue:1-2 Volume:273 Page:147-149
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Pagan Janet,Senior Alan E.

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(90)81071-U/fullpdf

Reference27 articles.

1. Properties of F1-ATPase from the uncD412 mutant of Escherichia coli

2. Specificity of the proton adenosine triphosphatase of Escherichia coli for adenine, guanine, and inosine nucleotides in catalysts and binding

3. ATP SYNTHASE (H+-ATPase): Results by Combined Biochemical and Molecular Biological Approaches

4. The Proton-Translocating ATPase of Escherichia Coli

5. Catalytic properties of the Escherichia coli proton adenosine triphosphatase: evidence that nucleotide bound at noncatalytic sites is not involved in regulation of oxidative phosphorylation

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