Article
Crystallographic analyses of NADH peroxidase Cys42Ala and Cys42Ser mutants: active site structures, mechanistic implications, and an unusual environment of Arg 303.
Biochemistry - 30 May 1995
Mande S S, Parsonage D, Claiborne A, Hol W G
Abstract excerpt
NADH peroxidase from Enterococcus faecalis is a tetrameric flavoenzyme of 201,400 Da which employs Cys 42 as a redox-active center cycling between sulfhydryl (Cys-SH) and sulfenic acid (Cys-SOH) states along the catalytic pathway. The role of the active site cysteine 42 in NADH peroxidase has bee...
Topics
- Alanine
- Arginine
- Binding Sites
- Catalysis
- Crystallography, X-Ray
- Cysteine
- Mutation
- Peroxidases
- Protein Structure, Tertiary
- Serine