高效生物催化 C-H 键氧化：一种来自热稳定细胞色素 P450 的工程化血红素硫醇加氧酶。
Efficient biocatalytic C-H bond oxidation: an engineered heme-thiolate peroxygenase from a thermostable cytochrome P450.
机构信息
School of Physics, Chemistry and Earth Sciences, University of Adelaide, Adelaide, SA 5005, Australia.
School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, Qld, 4072, Australia.
出版信息
Chem Commun (Camb). 2023 Nov 9;59(90):13486-13489. doi: 10.1039/d3cc04626e.
A 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 biocatalytic oxidation of C-H bonds at room temperature to 90 °C.
在化学合成中，人们非常追求的一个反应是激活未活化的碳-氢键。我们利用一种经过工程改造的耐热古菌细胞色素 P450 酶来实现脂肪酸的羟化。通过替换 I 螺旋的七个氨基酸部分，这个依赖烟酰胺辅酶的单加氧酶被转化为过氧化物酶，从而能够在室温至 90°C 的温度下，有效利用过氧酶将 C-H 键高效生物催化氧化。
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