Kayser Margaret M, Clouthier Christopher M
Department of Physical Sciences, University of New Brunswick, Saint John, New Brunswick, E2L 4L5 Canada.
J Org Chem. 2006 Oct 27;71(22):8424-30. doi: 10.1021/jo061349t.
Four mutants of the cyclohexanone monooxygenase (CHMO) evolved as catalysts for Baeyer-Villiger oxidation of 4-hydroxycyclohexanone were investigated as catalysts for a variety of 4-substituted and 4,4-disubstituted cyclohexanones. Several excellent catalytic matches (mutant/substrate) were identified. The most important, however, is the finding that, in a number of cases, a mutant with a single exchange, Phe432Ser, was shown to be as robust and more selective as a catalyst than the wild-type CHMO. All biotransformations were performed on a laboratory scale, allowing full characterization of the products. The absolute configurations of two products were established. A model suggesting a possible role of the 432 serine residue in enantioselectivity control is proposed.
研究了作为4-羟基环己酮的拜耳-维利格氧化反应催化剂而进化得到的环己酮单加氧酶（CHMO）的四个突变体，将其作为多种4-取代和4,4-二取代环己酮的催化剂。确定了几种优异的催化匹配（突变体/底物）。然而，最重要的是发现，在许多情况下，具有单一交换的突变体Phe432Ser作为催化剂比野生型CHMO更稳定且选择性更高。所有生物转化均在实验室规模上进行，从而能够对产物进行全面表征。确定了两种产物的绝对构型。提出了一个模型，表明432位丝氨酸残基在对映选择性控制中可能发挥的作用。
