Article
Structural Adaptability Facilitates Histidine Heme Ligation in a Cytochrome P450.
Journal of the American Chemical Society - 4 Nov 2015
McIntosh John A, Heel Thomas, Buller Andrew R, Chio Linda, Arnold Frances H
Abstract excerpt
Almost all known members of the cytochrome P450 (CYP) superfamily conserve a key cysteine residue that coordinates the heme iron. Although mutation of this residue abolishes monooxygenase activity, recent work has shown that mutation to either serine or histidine unlocks non-natural carbene- and nitrene-transfer activities. Here we present the first crystal structure of a histidine-ligated P450. The T213A/C317H...
Topics
- Archaeal Proteins
- Cytochrome P-450 Enzyme System
- Heme
- Histidine
- Models, Molecular
- Mutation
- Protein Conformation
- Sulfolobus acidocaldarius