Issue 16, 2009
From the journal:

Organic & Biomolecular Chemistry

Selective oxidation of aromatic sulfide catalyzed by an artificial metalloenzyme: new activity of hemozymes†

Rémy Ricoux,a   Mathieu Allard,a   Roger Dubuc,b   Claude Dupont,b   Jean-Didier Maréchalc  and  Jean-Pierre Mahy*a  

* Corresponding authors

a Institut de Chimie Moléculaire et des Matériaux d'Orsay, UMR 8182 CNRS, Laboratoire de Chimie Bioorganique et Bioinorganique, Bât. 420, Université Paris 11, Orsay Cedex, France
E-mail: jpmahy@icmo.u-psud.fr
Fax: +33(1)69157281
Tel: +33(1)69157421

b Institut National de la Recherche Scientifique, Institut Armand-Frappier, 531 Boulevard des Prairies, Laval, Québec, Canada

c Unitat de Química Física, Dep. de Química, Universitat Autònoma de Barcelona, Edifici C.n., Cerdonyola (Barcelona), Spain

Abstract

Two new artificial hemoproteins or “hemozymes”, obtained by non covalent insertion of Fe(III)-meso-tetra-p-carboxy- and -p-sulfonato-phenylporphyrin into xylanase A from Streptomyces lividans, were characterized by UV-visible spectroscopy and molecular modeling studies, and were found to catalyze the chemo- and stereoselective oxidation of thioanisole into the S sulfoxide, the best yield (85 ± 4%) and enantiomeric excess (40% ± 3%) being obtained with Fe(III)-meso-tetra-p-carboxyphenylporphyrin-Xln10A as catalyst in the presence of imidazole as co-catalyst.

Graphical abstract: Selective oxidation of aromatic sulfide catalyzed by an artificial metalloenzyme: new activity of hemozymes

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Article information

DOI
https://doi.org/10.1039/B907534H
Article type
Communication
Submitted
14 Apr 2009
Accepted
16 Jun 2009
First published
23 Jun 2009

Org. Biomol. Chem., 2009,7, 3208-3211

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Selective oxidation of aromatic sulfide catalyzed by an artificial metalloenzyme: new activity of hemozymes

R. Ricoux, M. Allard, R. Dubuc, C. Dupont, J. Maréchal and J. Mahy, Org. Biomol. Chem., 2009, 7, 3208 DOI: 10.1039/B907534H

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