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

Rémy Ricoux, Mathieu Allard, Roger Dubuc, Claude Dupont, Jean Didier Maréchal, Jean Pierre Mahy

Research output: Contribution to journalArticleResearchpeer-review

58 Citations (Scopus)

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. © The Royal Society of Chemistry 2009.
Original languageEnglish
Pages (from-to)3208-3211
JournalOrganic and Biomolecular Chemistry
Volume7
Issue number16
DOIs
Publication statusPublished - 1 Jan 2009

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