Girvan H M, Waltham T N, Neeli R, Collins H F, McLean K J, Scrutton N S, Leys D, Munro A W
Manchester Interdisciplinary Biocentre, School of Chemical Engineering and Analytical Science, University of Manchester, 131 Princess Street, Manchester M1 7ND, UK.
Biochem Soc Trans. 2006 Dec;34(Pt 6):1173-7. doi: 10.1042/BST0341173.
Flavocytochrome P450 (cytochrome P450) BM3 is an intensively studied model system within the P450 enzyme superfamily, and is a natural fusion of a P450 to its P450 reductase redox partner. The fusion arrangement enables efficient electron transfer within the enzyme and a catalytic efficiency that cannot be matched in P450 systems from higher organisms. P450 BM3's potential for industrially relevant chemical transformations is now recognized, and variants with biotechnological applications have been constructed. Simultaneously, structural and mechanistic studies continue to reveal the intricate mechanistic details of this enzyme, including its dimeric organization and the relevance of this quaternary structure to catalysis. Homologues of BM3 have been found in several bacteria and fungi, indicating important physiological functions in these microbes and enabling first insights into evolution of the enzyme family. This short paper deals with recent developments in our understanding of structure, function, evolution and biotechnological applications of this important P450 system.
黄素细胞色素P450（细胞色素P450）BM3是P450酶超家族中一个经过深入研究的模型系统，它是一种P450与其P450还原酶氧化还原伴侣的天然融合体。这种融合结构使得酶内能够进行高效的电子转移，并且具有较高的催化效率，这是高等生物的P450系统所无法比拟的。现在人们已经认识到P450 BM3在工业相关化学转化方面的潜力，并且构建了具有生物技术应用价值的变体。与此同时，结构和机理研究不断揭示该酶复杂的机理细节，包括其二聚体结构以及这种四级结构与催化作用的相关性。在几种细菌和真菌中发现了BM3的同源物，这表明该酶在这些微生物中具有重要的生理功能，并且有助于初步了解该酶家族的进化情况。这篇短文论述了我们在理解这个重要的P450系统的结构、功能、进化和生物技术应用方面的最新进展。
