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. © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
- Artificial metalloenzymes
- Asymmetric catalysis