Hydroperoxide-dependent sulfoxidation catalyzed by soybean microsomes.
The sulfoxidation of methiocarb, an aromatic-alkyl sulfide pesticide, catalyzed by soybean microsomes was found to be strongly stimulated in the presence of cumene and linoleic acid hydroperoxides. We have shown that this S-oxidation, which does not require cofactors such as NAD(P)H, is an hydroperoxide-dependent reaction: 18O2-labeling experiments demonstrated that the oxygen atom incorporated into the sulfoxide originated from hydroperoxides rather than from molecular oxygen. In the absence of exogenous hydroperoxides, soybean microsomes catalyzed methiocarb sulfoxide formation at a basal rate dependent on their endogenous hydroperoxides, especially those derived from free fatty acids. The nature of the sulfoxidase is discussed. Our results seem to rule out the participation of cytochrome P-450 in this oxidation, whereas the studied sulfoxidase presents some similarities to plant peroxygenase.
D001555:Benzene Derivatives / Q000494:pharmacology; D008054:Lipid Peroxides / Q000378:metabolism; D008714:Methiocarb / Q000378:metabolism; D008861:Microsomes / Q000378:metabolism; D006899:Mixed Function Oxygenases / Q000378:metabolism; D010545:Peroxides / Q000378:metabolism*; D010944:Plants / Q000378:metabolism*; D013025:Glycine max / Q000378:metabolism; D013454:Sulfoxides / Q000378:metabolism*
D001555:Benzene Derivatives; D008054:Lipid Peroxides; D010545:Peroxides; D013454:Sulfoxides; D006899:Mixed Function Oxygenases; C022333:peroxygenase; D008714:Methiocarb; C007164:cumene hydroperoxide