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

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.
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Submitted on : Thursday, May 2, 2013 - 4:25:33 AM
Last modification on : Saturday, June 25, 2022 - 10:10:03 PM

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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 and Biomolecular Chemistry, Royal Society of Chemistry, 2009, 7 (16), pp.3208-11. ⟨10.1039/b907534h⟩. ⟨pasteur-00819650⟩

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