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Issue 16, 2009
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Selective oxidation of aromatic sulfide catalyzed by an artificial metalloenzyme: new activity of hemozymes

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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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Publication details

The article was received on 14 Apr 2009, accepted on 16 Jun 2009, published on 23 Jun 2009 and first published online on 23 Jun 2009


Article type: Communication
DOI: 10.1039/B907534H
Citation: 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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