Abstract
A specific b subunit arginine, b(Arg-36) in Escherichia coli, displays evolutionary conservation among bacterial F1F0 ATP synthases. Site- directed mutagenesis was used to generate a collection of mutations affecting b(Arg-36). The phenotype differed depending upon the substitution, and the b(Arg-36→Glu) and b(Arg-36→Ile) substitutions virtually abolished enzyme function. Although the total amounts of F1F0 ATP synthase present in the membranes prepared from mutant strains were reduced, the primary effect of the b(Arg-36) substitutions was on the activities of the intact enzyme complexes. The most interesting result was that the b(Arg-36-Glu) substitution results in the uncoupling of a functional F0 from F1 ATP hydrolysis activity.
Original language | English (US) |
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Pages (from-to) | 201-206 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 429 |
Issue number | 2 |
DOIs | |
State | Published - Jun 12 1998 |
Externally published | Yes |
Keywords
- FF ATP synthase
- Proton translocation
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology