Article
Active site of mercuric reductase resides at the subunit interface and requires Cys135 and Cys140 from one subunit and Cys558 and Cys559 from the adjacent subunit: evidence from in vivo and in vitro heterodimer formation.
Biochemistry - 20 Mar 1990
Distefano M D, Moore M J, Walsh C T
Abstract excerpt
Mercuric reductase catalyzes the two-electron reduction of Hg(II) to Hg(0) using NADPH as the reductant; this reaction constitutes the molecular basis for detoxification of Hg(II) by bacteria. The enzyme is an alpha 2 homodimer and possesses two pairs of cysteine residues, Cys135 and Cys140 (redo...
Topics
- Base Sequence
- Binding Sites
- Catalysis
- Cysteine
- DNA
- Erythrocytes
- Escherichia coli
- Genetic Complementation Test
- Humans
- Mutation
- Oxidation-Reduction
- Oxidoreductases
- Promoter Regions, Genetic
- Protein Conformation