Structure of a cytochrome P450-redox partner electron-transfer complex
Structure of a cytochrome P450-redox partner electron-transfer complex
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DOI：
10.1073/pnas.96.5.1863
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发表时间：
1999-03-02
影响因子：
11.1
通讯作者：
Poulos, TL
中科院分区：
文献类型：
--
作者：
Sevrioukova, IF;Li, HY;Poulos, TL
细菌细胞色素 P450BM-3 的血红素和 FMN 结合域之间的复合物（真核微粒体 P450 和 P450 还原酶之间的复合物的原型）的晶体结构已在 2.03 埃分辨率下测定。黄素氧还蛋白样黄素结构域位于血红素结构域的近端面，FMN 分别距血红素结合环和血红素铁之前的肽 4.0 和 18.4 埃。血红素结合肽代表了通往血红素铁的最有效且耦合的键合电子途径。在黄素结合位点周围观察到，P450BM-3 和微粒体 P450 还原酶的 FMN 结合域之间存在显着差异，这导致了 FMN 不同的氧化还原特性，进而控制流向 P450 的电子流。
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 Angstrom resolution. The flavodoxin-like flavin domain is positioned at the proximal face of the heme domain with the FMN 4.0 and 18.4 Angstrom 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.