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J Bacteriol. 1992 January; 174(2): 633-637
| research-article |
Department of Biological Sciences, Southern Methodist University, Dallas, Texas 75275-0376.
ABSTRACT
A collection of amino acid substitutions at residues Glu-32 and His-39 in the epsilon subunit of the Escherichia coli F1F0 ATP synthase has been constructed by cassette mutagenesis. Substitutions for residue Glu-32 appeared to cause abnormal inhibition of membrane-bound F1 ATPase activity, and replacement of His-39 by Arg, Val, and Pro affected F1F0 interactions.
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