Adenine nucleotide binding sites in normal and mutant adenosine triphosphatases of Escherichia coli
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference27 articles.
1. Membrane Adenosine Triphosphatases of Prokaryotic Cells
2. Structure of oxidative- and photo-phosphorylation coupling factor complexes
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4. The uncA gene codes for the α-subunit of the adenosine triphosphatase of Escherichia coli. Electrophoretic analysis of uncA mutant strains
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1. Peptide analogs of the beef heart mitochondrial F1-ATPase inhibitor protein;Biochemistry;1993-07
2. 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
3. The binding change mechanism for ATP synthase — Some probabilities and possibilities;Biochimica et Biophysica Acta (BBA) - Bioenergetics;1993-01
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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