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Incorporation of Manganese Complexes into Xylanase: New Artificial Metalloenzymes for Enantioselective Epoxidation
Author(s) -
Allard Mathieu,
Dupont Claude,
Muñoz Robles Victor,
Doucet Nicolas,
Lledós Agustí,
Maréchal JeanDidier,
Urvoas Agathe,
Mahy JeanPierre,
Ricoux Rémy
Publication year - 2012
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201100659
Subject(s) - chemistry , circular dichroism , enantioselective synthesis , manganese , catalysis , styrene , artificial enzyme , porphyrin , yield (engineering) , stereochemistry , combinatorial chemistry , copolymer , organic chemistry , polymer , materials science , metallurgy
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(T p CPP), 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.