Selective oxidation of aromatic sulfide catalyzed by an artificial metalloenzyme: new activity of hemozymes.
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.
Ricoux
Rémy
R
Institut de Chimie Moléculaire et des Matériaux d'Orsay, UMR 8182 CNRS, Laboratoire de Chimie Bioorganique et Bioinorganique, Bât. 420, Université Paris 11, 91405, Orsay Cedex, France.
Allard
Mathieu
M
Dubuc
Roger
R
Dupont
Claude
C
Maréchal
Jean-Didier
JD
Mahy
Jean-Pierre
JP
D002384:Catalysis; D008667:Metalloproteins / Q000737:chemistry*; D015394:Molecular Structure; D010084:Oxidation-Reduction; D010100:Oxygen / Q000737:chemistry*; D013440:Sulfides / Q000737:chemistry*; D013454:Sulfoxides / Q000737:chemistry
D008667:Metalloproteins; D013440:Sulfides; D013454:Sulfoxides; C093850:methylphenylsulfide; D010100:Oxygen