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1: Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):1863-8.Click here to read Click here to read Links

Structure of a cytochrome P450-redox partner electron-transfer complex.

Sevrioukova IF, Li H, Zhang H, Peterson JA, Poulos TL.

University of California, Department of Molecular Biology and Biochemistry, 3205 Bio Sci II, Irvine, CA 92697-3900, USA.

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 A resolution. The flavodoxin-like flavin domain is positioned at the proximal face of the heme domain with the FMN 4.0 and 18.4 A 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.

PMID: 10051560 [PubMed - indexed for MEDLINE]

PMCID: PMC26702

Structures reported by this article