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.
journal_name
Proc Natl Acad Sci U S Aauthors
Sevrioukova IF,Li H,Zhang H,Peterson JA,Poulos TLdoi
10.1073/pnas.96.5.1863keywords:
subject
Has Abstractpub_date
1999-03-02 00:00:00pages
1863-8issue
5eissn
0027-8424issn
1091-6490journal_volume
96pub_type
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