细胞色素P450-氧化还原伴侣电子传递复合物的结构。
Structure of a cytochrome P450-redox partner electron-transfer complex.
作者信息
Sevrioukova I F, Li H, Zhang H, Peterson J A, Poulos T L
机构信息
University of California, Department of Molecular Biology and Biochemistry, 3205 Bio Sci II, Irvine, CA 92697-3900, USA.
出版信息
Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):1863-8. doi: 10.1073/pnas.96.5.1863.
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.
摘要
细菌细胞色素P450BM-3的血红素结合域与黄素单核苷酸（FMN）结合域之间复合物的晶体结构已在2.03埃分辨率下测定。细胞色素P450BM-3是真核微粒体P450与P450还原酶之间复合物的原型。类黄素氧还蛋白的黄素结构域位于血红素结构域的近侧面，FMN分别距离血红素结合环之前的肽段和血红素铁4.0埃和18.4埃。血红素结合肽代表了与血红素铁最有效且通过键连接的电子传递途径。在黄素结合位点周围观察到的P450BM-3和微粒体P450还原酶的FMN结合域之间的显著差异，导致了FMN不同的氧化还原特性，进而控制了向P450的电子流动。
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