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J Bacteriol. 1992 January; 174(2): 633-637

research-article

Mutations at Glu-32 and His-39 in the epsilon subunit of the Escherichia coli F1F0 ATP synthase affect its inhibitory properties.

D J LaRoe and S B Vik

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.


J Bacteriol. 1992 January; 174(2): 633-637




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