Institut de Chimie Moléculaire et des Matériaux d'Orsay, UMR 8182 CNRS, Laboratoire de Chimie Bioorganique et Bioinorganique, Bâtiment 420, Université Paris XI, 91405 Orsay Cedex, France.
Chembiochem. 2012 Jan 23;13(2):240-51. doi: 10.1002/cbic.201100659. Epub 2011 Dec 21.
Here we report the best artificial metalloenzyme to date for the selective oxidation of aromatic alkenes; it was obtained by noncovalent insertion of Mn(III)-meso-tetrakis(p-carboxyphenyl)porphyrin [Mn(TpCPP), 1-Mn] into a host protein, xylanase 10A from Streptomyces lividans (Xln10A). Two metallic complexes-N,N'-ethylene bis(2-hydroxybenzylimine)-5,5'-dicarboxylic acid Mn(III) [(Mn-salen), 2-Mn] and 1-Mn-were associated with Xln10A, and the two hybrid biocatalysts were characterised by UV-visible spectroscopy, circular dichroism and molecular modelling. Only the artificial metalloenzyme based on 1-Mn and Xln10A was studied for its catalytic properties in the oxidation of various substituted styrene derivatives by KHSO(5): after optimisation, the 1-Mn-Xln10A artificial metalloenzyme was able to catalyse the oxidation of para-methoxystyrene by KHSO(5) with a 16 % yield and the best enantioselectivity (80 % in favour of the R isomer) ever reported for an artificial metalloenzyme.
在这里，我们报道了迄今为止用于芳香烯烃选择性氧化的最佳人工金属酶；它是通过非共价插入 Mn(III)-meso-四(对羧基苯基)卟啉[Mn(TpCPP)，1-Mn]到宿主蛋白木聚糖酶 10A（来自链霉菌属 lividans 的 Xln10A）中获得的。两种金属配合物-N,N'-亚乙基双（2-羟基苯甲亚胺）-5,5'-二羧酸 Mn(III)[(Mn-salen)，2-Mn]和 1-Mn 与 Xln10A 结合，并用紫外-可见光谱、圆二色性和分子建模对两种杂交生物催化剂进行了表征。只有基于 1-Mn 和 Xln10A 的人工金属酶在通过 KHSO(5)氧化各种取代的苯乙烯衍生物的催化性能方面进行了研究：经过优化，1-Mn-Xln10A 人工金属酶能够以 16%的产率和有史以来报道的最高对映选择性（80%有利于 R 异构体）催化 KHSO(5)对对甲氧基苯乙烯的氧化。
