Allard, Mathieu; Dupont, Claude; Munoz Robles, Victor; Doucet, Nicolas 
ORCID: https://orcid.org/0000-0002-1952-9380; Lledos, Agusti; Marechal, Jean-Didier; Urvoas, Agathe; Mahy, Jean-Pierre et Ricoux, Remy
(2012).
Incorporation of manganese complexes into xylanase: new artificial metalloenzymes for enantioselective epoxidation
Chembiochem
, vol. 13
, nº 2.
pp. 240-51.
DOI: 10.1002/cbic.201100659.
Résumé
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.
| Type de document: | Article |
|---|---|
| Mots-clés libres: | - |
| Centre: | Centre INRS-Institut Armand Frappier |
| Date de dépôt: | 04 mars 2024 16:18 |
| Dernière modification: | 04 mars 2024 16:18 |
| URI: | https://espace.inrs.ca/id/eprint/13975 |
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