Article
The role of distal tryptophan in the bifunctional activity of catalase-peroxidases.
Biochemical Society transactions - 1 May 2001
Regelsberger G, Jakopitsch C, Furtmüller P G, Rueker F, Switala J, Loewen P C, Obinger C
Abstract excerpt
Catalase-peroxidases are bifunctional peroxidases exhibiting an overwhelming catalase activity and a substantial peroxidase activity. Here we present a kinetic study of the formation and reduction of the key intermediate compound I by probing the role of the conserved tryptophan at the distal haem cavity site. Two wild-type proteins and three mutants of Synechocystis catalase-peroxidase (W122A and W122F) and...
Topics
- Bacterial Proteins
- Binding Sites
- Catalysis
- Cyanobacteria
- Cytochrome-c Peroxidase
- Escherichia coli
- Heme
- Hydrogen Peroxide
- Kinetics
- Multienzyme Complexes
- Mutation
- Oxidation-Reduction
- Peroxidases
- Protein Binding
- Spectrophotometry
- Tryptophan
- Yeasts