Selective oxidation of aromatic sulfide catalyzed by an artificial metalloenzyme: new activity of hemozymes. - Archive ouverte HAL Access content directly
Journal Articles Organic & Biomolecular Chemistry Year : 2009

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.

Dates and versions

pasteur-00819650 , version 1 (02-05-2013)

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Rémy Ricoux, Mathieu Allard, Roger Dubuc, Claude Dupont, Jean-Didier Maréchal, et al.. Selective oxidation of aromatic sulfide catalyzed by an artificial metalloenzyme: new activity of hemozymes.. Organic & Biomolecular Chemistry, 2009, 7 (16), pp.3208-11. ⟨10.1039/b907534h⟩. ⟨pasteur-00819650⟩
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