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

Irina F. Sevrioukova, Huiying Li, Hong Zhang, Julian A. Peterson, Thomas L. Poulos

Research output: Contribution to journalArticle

398 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)1863-1868
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume96
Issue number5
DOIs
StatePublished - Mar 2 1999

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Keywords

  • Cytochrome P450 reductase, flavodoxin
  • Protein-protein interaction

ASJC Scopus subject areas

  • General

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