Article
Temperature-jump relaxation kinetics of substrate-induced spin-state transition in cytochrome P450 (comparison of the wild-type and C334A mutant P450(CAM) and P450(2B4)).
Archives of biochemistry and biophysics - 15 Apr 2001
Narasimhulu S, Willcox J K
Abstract excerpt
The kinetics of binding of the substrate camphor to the cytochrome P450(CAM) and the C334A mutant as well as the kinetics of binding of benzphetamine to the wild-type P450(2B4) have been studied by the temperature-jump relaxation technique in order to distinguish between the two models for substrate-induced spin-state transition. These models are the bimolecular model in which spin-state transition occurs in...
Topics
- Amino Acid Substitution
- Cytochrome P-450 Enzyme System
- Kinetics
- Models, Molecular
- Mutation
- Substrate Specificity
- Temperature