Oxidation of aromatic sulfides by lignin peroxidase from Phanerochaete chrysosporium.
The reaction of H2O2 with 4-substituted aryl alkyl sulfides (4-XC6H4SR), catalysed by lignin peroxidase (LiP) from Phanerochaete chrysosporium, leads to the formation of sulfoxides, accompanied by diaryl disulfides. The yields of sulfoxide are greater than 95% when X = OMe, but decrease significantly as the electron donating power of the substituent decreases. No reaction is observed for X = CN. The bulkiness of the R group has very little influence on the efficiency of the reaction, except for R = tBu. The reaction exhibits enantioselectivity (up to 62% enantiomeric excess with X = Br, with preferential formation of the sulfoxide with S configuration). Enantioselectivity decreases with increasing electron density of the sulfide. Experiments in H218O show partial or no incorporation of the labelled oxygen into the sulfoxide, with the extent of incorporation decreasing as the ring substituents become more electron-withdrawing. On the basis of these results, it is suggested that LiP compound I (formed by reaction between the native enzyme and H2O2), reacts with the sulfide to form a sulfide radical cation and LiP compound II. The radical cation is then converted to sulfoxide either by reaction with the medium or by a reaction with compound II, the competition between these two pathways depending on the stability of the radical cation.
Baciocchi
E
E
Dipartimento di Chimica, Universitá di Roma 'La Sapienza', Italy. baciocchi@axcasp.caspur.it
Gerini
M F
MF
Harvey
P J
PJ
Lanzalunga
O
O
Mancinelli
S
S
D010084:Oxidation-Reduction; D010544:Peroxidases / Q000378:metabolism*; D020075:Phanerochaete / Q000201:enzymology*; D013440:Sulfides / Q000378:metabolism*
D013440:Sulfides; D010544:Peroxidases; C042858:lignin peroxidase