Article
Multiple pathways of electron transfer in dimethyl sulfoxide reductase of Escherichia coli.
The Journal of biological chemistry - 11 Mar 1994
Trieber C A, Rothery R A, Weiner J H
Abstract excerpt
The catalytic subunit of dimethyl sulfoxide (Me2SO) reductase, DmsA, contains six blocks of sequence that are homologous to other members of the superfamily of prokaryotic molybdoenzymes. The amino-terminal block contains 5 conserved residues (Cys38, Cys42, Cys75, Lys28, and Arg77). Site-directed mutagenesis of these residues did not alter membrane localization but in some cases less enzyme accumulated. The...
Topics
- Amino Acid Sequence
- Base Sequence
- Electron Transport
- Escherichia coli
- Iron-Sulfur Proteins
- Molecular Sequence Data
- Mutation
- Naphthols
- Oligodeoxyribonucleotides
- Oxidation-Reduction
- Oxidoreductases