Structure of a cytochrome P450–redox partner electron-transfer complex
AUTOR(ES)
Sevrioukova, Irina F.
FONTE
The National Academy of Sciences
RESUMO
The crystal structure of the complex between the heme- and FMN-binding domains of bacterial cytochrome P450BM-3, a prototype for the complex between eukaryotic microsomal P450s and P450 reductase, has been determined at 2.03 Å resolution. The flavodoxin-like flavin domain is positioned at the proximal face of the heme domain with the FMN 4.0 and 18.4 Å from the peptide that precedes the heme-binding loop and the heme iron, respectively. The heme-binding peptide represents the most efficient and coupled through-bond electron pathway to the heme iron. Substantial differences between the FMN-binding domains of P450BM-3 and microsomal P450 reductase, observed around the flavin-binding sites, are responsible for different redox properties of the FMN, which, in turn, control electron flow to the P450.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=26702Documentos Relacionados
- Structure of an intermolecular electron-transfer complex: p-cresol methylhydroxylase at 6.0-A resolution.
- Electrostatic effects on electron-transfer kinetics in the cytochrome f-plastocyanin complex.
- A redox-dependent interaction between two electron-transfer partners involved in photosynthesis
- The currents of life: the terminal electron-transfer complex of respiration.
- Electron-transfer functionality of synthetic coiled-coil metalloproteins