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Incorporation of manganese complexes into xylanase: new artificial metalloenzymes for enantioselective epoxidation.

Abstract : 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.
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https://hal-riip.archives-ouvertes.fr/pasteur-00736965
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Submitted on : Monday, October 1, 2012 - 5:02:51 AM
Last modification on : Wednesday, September 16, 2020 - 5:05:08 PM

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Mathieu Allard, Claude Dupont, Victor Muñoz Robles, Nicolas Doucet, Agustí Lledós, et al.. Incorporation of manganese complexes into xylanase: new artificial metalloenzymes for enantioselective epoxidation.. ChemBioChem, Wiley-VCH Verlag, 2012, 13 (2), pp.240-51. ⟨10.1002/cbic.201100659⟩. ⟨pasteur-00736965⟩

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