ELECTRON TRANSFER COMPLEXES BETWEEN CYTOCHROME P450 W/ THEIR REDOX PARTNERS

细胞色素P450酶催化多种反应，例如 药物和致癌物的解毒，类固醇的生物合成 激素、维生素激活等。电子，氧化所需 的基质，被输送到P450的铁硫或 蛋白质或含FAD/FMN的NADPH-细胞色素P450还原酶。 如何 P450与它们的氧化还原伙伴相互作用， 电子转移是分子机制和功能的关键问题， P450酶。 细胞色素P450 BM-3的可溶性融合蛋白 由血红素和还原酶结构域组成， 多肽链，是研究P450-P450还原酶的最佳模型 交互. 我们结晶了这种酶的75 kDa片段， 由血红素和FMN结合结构域组成。 大晶胞 而使用内部X射线源获得的衍射图较差， 不允许我们改进这个结构。

Cytochrome P450 enzymes catalyze a variety of reactions, such as detoxication of drugs and carcinogens, biosynthesis of steroid hormones, vitamin activation, etc. Electrons, required for oxidation of substrates, are being delivered to P450s by either iron-sulfur proteins or FAD/FMN-containing NADPH-cytochrome P450 reductase. How P450s interact with their redox partners and what is the mechanism of electron transfer are the key questions in mechanism and function of P450 enzymes. Cytochrome P450BM-3, a soluble fusion protein consisting of both the heme- and reductase domains on a single polypeptide chain, is the best model for studying P450-P450 reductase interactions. We crystallized a 75 kDa fragment of this enzyme, consisting of both the heme- and FMN-binding domains. Large unit cell and poor diffraction pattern, obtained using in-house X-ray source, do not allow us to refine this structure.