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PMID: 6457039 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

The defective proton-ATPase of uncA mutants of Escherichia coli. Studies of nucleotide binding sites, bound aurovertin fluorescence, and labeling of essential residues of the purified F1-ATPase.

The Journal of biological chemistry ·Vol. 256 ·No. 20 ·1981-10-25 ·Pages 10383-9

Wise JG, Latchney LR, Senior AE

Abstract

暂无摘要

MeSH Terms
Adenosine Diphosphate Adenosine Triphosphatases/metabolism Aurovertins Binding Sites Cell Membrane/enzymology Escherichia coli/enzymology Genotype Kinetics Mutation Oxidative Phosphorylation Coupling Factors/metabolism Protein Binding Proton-Translocating ATPases Pyrans Species Specificity Spectrometry, Fluorescence
Chemicals
Aurovertins Oxidative Phosphorylation Coupling Factors Pyrans Adenosine Diphosphate Adenosine Triphosphatases Proton-Translocating ATPases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Wise J G
Latchney L R
Senior A E
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1981-10-25
Pages
10383-9
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NIGMS NIH HHS · GM-25349 · United States
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