Article
Cysteinyl and substrate radical formation in active site mutant E441Q of Escherichia coli class I ribonucleotide reductase.
The Journal of biological chemistry - 20 Nov 1998
Persson A L, Sahlin M, Sjöberg B M
Abstract excerpt
All classes of ribonucleotide reductase are proposed to have a common reaction mechanism involving a transient cysteine thiyl radical that initiates catalysis by abstracting the 3'-hydrogen atom of the substrate nucleotide. In the class Ia ribonucleotide reductase system of Escherichia coli, we r...
Topics
- Catalytic Domain
- Cysteine
- Cytidine Diphosphate
- Electron Spin Resonance Spectroscopy
- Escherichia coli
- Free Radicals
- Models, Chemical
- Mutation
- Ribonucleotide Reductases
- Spin Trapping