Non-covalently bound adenine nucleotides in adenosine triphosphatase of Escherichiacoli
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference28 articles.
1. Tight binding of adenine nucleotides to beef-heart mitochondrial ATPase
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4. Tightly bound adenine nucleotide in bacterial membrane ATPase
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1. 3′-O-(4-Benzoyl)benzoyladenosine 5′-Triphosphate Inhibits Activity of the Vacuolar (H+)-ATPase from Bovine Brain Clathrin-coated Vesicles by Modification of a Rapidly Exchangeable, Noncatalytic Nucleotide Binding Site on the B Subunit;Journal of Biological Chemistry;1996-05
2. Influence of nucleotide binding site occupancy on the thermal stability of the F1 portion of the chloroplast ATP synthase.;Journal of Biological Chemistry;1993-10
3. The Effect of Depletion of Nucleotide and of δ and ϵ Subunits on ATP Synthesis in Dimethyl Sulfoxide by F1-ATPase of Escherichia coli;Biochemical and Biophysical Research Communications;1993-07
4. Escherichia coli F1-ATPase can use GTP-nonchaseable bound adenine nucleotide to synthesize ATP in dimethyl sulfoxide;Biochemistry;1992-11-01
5. Changes in the adenine nucleotide and inorganic phosphate content of Escherichia coli F1-ATPase during ATP synthesis in dimethyl sulphoxide;Biochemical Journal;1992-09-01
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