Department of Chemistry, San José State University , One Washington Square, San José, California 95192-0101, United States.
J Am Chem Soc. 2013 Oct 2;135(39):14484-7. doi: 10.1021/ja409337v. Epub 2013 Sep 19.
P450s are heme thiolate enzymes that catalyze the regio- and stereoselective functionalization of unactivated C-H bonds using molecular dioxygen and two electrons delivered by the reductase. We have developed hybrid P450 BM3 heme domains containing a covalently attached Ru(II) photosensitizer in order to circumvent the dependency on the reductase and perform P450 reactions upon visible light irradiation. A highly active hybrid enzyme with improved stability and a modified Ru(II) photosensitizer is able to catalyze the light-driven hydroxylation of lauric acid with total turnover numbers of 935 and initial reaction rate of 125 mol product/(mol enzyme/min).
P450s 是含血红素硫醚酶，使用分子氧和还原酶提供的两个电子，催化未活化的 C-H 键的区域和立体选择性功能化。我们已经开发了含有共价连接的 Ru(II)光敏剂的杂交 P450 BM3 血红素结构域，以避免对还原酶的依赖，并在可见光照射下进行 P450 反应。一种具有高活性、改进的稳定性和改良的 Ru(II)光敏剂的杂交酶能够催化月桂酸的光驱动羟基化，总周转率为 935，初始反应速率为 125 mol 产物/(mol 酶/min)。
