Selective aliphatic carbon–hydrogen bond activation of protected alcohol substrates by cytochrome P450 enzymes

…, JTJ Spence, S Liu, JH George, LL Wong

文献索引：Bell, Stephen G.; Spence, Justin T. J.; Liu, Shenglan; George, Jonathan H.; Wong, Luet-Lok Organic and Biomolecular Chemistry, 2014 , vol. 12, # 15 p. 2479 - 2488

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被引用次数: 3

摘要

Protected cyclohexanol and cyclohex-2-enol substrates, containing benzyl ether and benzoate ester moieties, were designed to fit into the active site of the Tyr96Ala mutant of cytochrome P450cam. The protected cyclohexanol substrates were efficiently and selectively hydroxylated by the mutant enzyme at the trans C–H bond of C-4 on the cyclohexyl ring. The selectivity of oxidation of the benzoate ester protected cyclohexanol ...