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

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 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.

authors

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

doi

10.1073/pnas.96.5.1863

keywords:

subject

Has Abstract

pub_date

1999-03-02 00:00:00

pages

1863-8

issue

5

eissn

0027-8424

issn

1091-6490

journal_volume

96

pub_type

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