Efficient biocatalytic C–H bond oxidation: an engineered heme-thiolate peroxygenase from a thermostable cytochrome P450
作者:Alecia R. Gee、Isobella S. J. Stone、Tegan P. Stockdale、Tara L. Pukala、James J. De Voss、Stephen G. Bell
DOI:10.1039/d3cc04626e
日期:——
highly sought after reaction in chemical synthesis is the activation of unactivated carbon–hydrogen bonds. We demonstrate the hydroxylation of fatty acids using an engineered thermostable archaeal cytochrome P450 enzyme. By replacing a seven amino acid section of the I-helix, the nicotinamide cofactor-dependent monooxygenase was converted into a hydrogen peroxide using peroxygenase, enabling the efficient
化学合成中备受追捧的反应是未活化的碳氢键的活化。我们使用工程化的热稳定古菌细胞色素 P450 酶演示了脂肪酸的羟基化。通过替换 I 螺旋的 7 个氨基酸部分,烟酰胺辅因子依赖性单加氧酶使用过加氧酶转化为过氧化氢,从而能够在室温至 90 °C 下对 C-H 键进行有效的生物催化氧化。