Open AccessMutations at Glu-32 and His-39 in the epsilon subunit of the Escherichia coli F1F0 ATP synthase affect its inhibitory properties
Author(s) -
D J LaRoe,
Steven B. Vik
Publication year - 1992
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.174.2.633-637.1992
Subject(s) - biology , escherichia coli , atp synthase , protein subunit , biochemistry , mutagenesis , atpase , microbiology and biotechnology , atp synthase gamma subunit , enzyme , mutation , gene , atp hydrolysis
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.