Article
Use of a site-directed triple mutant to trap intermediates: demonstration that the flavin C(4a)-thiol adduct and reduced flavin are kinetically competent intermediates in mercuric ion reductase.
Biochemistry - 20 Mar 1990
Miller S M, Massey V, Ballou D, Williams C H, Distefano M D, Moore M J, Walsh C T
Abstract excerpt
A mutant form of mercuric reductase, which has three of its four catalytically essential cysteine residues replaced by alanines (ACAA: Ala135Cys140Ala558Ala559), has been constructed and used for mechanistic investigations. With disruption of the Hg(II) binding site, the mutant enzyme is devoid o...
Topics
- Amino Acid Sequence
- Base Sequence
- Escherichia coli
- Flavin-Adenine Dinucleotide
- Flavins
- Hydrogen-Ion Concentration
- Kinetics
- Molecular Sequence Data
- Mutation
- NAD
- Oxidation-Reduction
- Oxidoreductases
- Sulfhydryl Compounds