Munro Andrew W, Girvan Hazel M, McLean Kirsty J
Manchester Interdisciplinary Biocentre, School of Chemical Engineering and Analytical Science, University of Manchester, 131 Princess Street, Manchester, M1 7ND, UK.
Biochim Biophys Acta. 2007 Mar;1770(3):345-59. doi: 10.1016/j.bbagen.2006.08.018. Epub 2006 Aug 30.
The cytochromes P450 (P450s) are a broad class of heme b-containing mono-oxygenase enzymes. The vast majority of P450s catalyse reductive scission of molecular oxygen using electrons usually derived from coenzymes (NADH and NADPH) and delivered from redox partner proteins. Evolutionary advantages may be gained by fusion of one or more redox partners to the P450 enzyme in terms of e.g. catalytic efficiency. This route was taken by the well characterized flavocytochrome P450(BM3) system (CYP102A1) from Bacillus megaterium, in which soluble P450 and cytochrome P450 reductase enzymes are covalently linked to produce a highly efficient electron transport system for oxygenation of fatty acids and related molecules. However, genome analysis and ongoing enzyme characterization has revealed that there are a number of other novel classes of P450-redox partner fusion enzymes distributed widely in prokaryotes and eukaryotes. This review examines our current state of knowledge of the diversity of these fusion proteins and explores their structural composition and evolutionary origins.
细胞色素P450（P450s）是一类含血红素b的广泛的单加氧酶。绝大多数P450利用通常来自辅酶（NADH和NADPH）并由氧化还原伴侣蛋白传递的电子催化分子氧的还原裂解。就催化效率等方面而言，将一个或多个氧化还原伴侣与P450酶融合可能会带来进化优势。巨大芽孢杆菌中特征明确的黄素细胞色素P450（BM3）系统（CYP102A1）就采用了这种途径，其中可溶性P450和细胞色素P450还原酶通过共价连接形成一个高效的电子传递系统，用于脂肪酸及相关分子的氧化。然而，基因组分析和正在进行的酶特性研究表明，在原核生物和真核生物中广泛分布着许多其他新型的P450-氧化还原伴侣融合酶。本文综述了我们目前对这些融合蛋白多样性的认识，并探讨了它们的结构组成和进化起源。
