TY - JOUR
T1 - Structure of a cytochrome P450-redox partner electron-transfer complex
AU - Sevrioukova, Irina F.
AU - Li, Huiying
AU - Zhang, Hong
AU - Peterson, Julian A.
AU - Poulos, Thomas L.
PY - 1999/3/2
Y1 - 1999/3/2
N2 - 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.
AB - 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.
KW - Cytochrome P450 reductase, flavodoxin
KW - Protein-protein interaction
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U2 - 10.1073/pnas.96.5.1863
DO - 10.1073/pnas.96.5.1863
M3 - Article
C2 - 10051560
AN - SCOPUS:0033514990
SN - 0027-8424
VL - 96
SP - 1863
EP - 1868
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 5
ER -