Oxidation of dimethyl sulfide by various aromatic compound oxygenases frombacteria

As a result of the determination of dimethyl sulfide (DMS) oxidizing activi ty of bacterial aromatic compound oxygenases, multicomponent monooxygenases (DmpKLMNOP from Pseudomonas sp. CF600, AphKLMNOP from Comamonas testostero ni TA441, and TodABCDEF from Pseudomonas sp. JS150), single component monoo xygenases (TfdB from Pseudomonas putida EST4011 and XylMA from Pseudomonas putida mt-2), and dioxygenases (CumA1A2A3A4 from Pseudomonas fluorescens IP 01 and PahAaAbAcAd from Pseudomonas putida OUS82) showed DMS-oxidizing acti vity, while CarAaAcAd from Pseudomonas sp. CA10 and SoxC from Rhodococcus s p. IGTS8 did not. These results indicate the possibilities that these oxyge nases might oxidize DMS to DMSO under the natural condition in the environm ent.