Pt. Visscher et Bf. Taylor, A NEW MECHANISM FOR THE AEROBIC CATABOLISM OF DIMETHYL SULFIDE, Applied and environmental microbiology, 59(11), 1993, pp. 3784-3789
Aerobic degradation of dimethyl sulfide (DMS), previously described fo
r thiobacilli and hyphomicrobia, involves catabolism to sulfide via me
thanethiol (CH3SH). Methyl groups are sequentially eliminated as HCHO
by incorporation of O2 catalyzed by DMS monooxygenase and methanethiol
oxidase. H2O2 formed during CH3SH oxidation is destroyed by catalase.
We recently isolated Thiobacillus strain ASN-1, which grows either ae
robically or anaerobically with denitrification on DMS. Comparative ex
periments with Thiobacillus thioparus T5, which grows only aerobically
on DMS, indicate a novel mechanism for aerobic DMS catabolism by Thio
bacillus strain ASN-1. Evidence that both organisms initially attacked
the methyl group, rather than the sulfur atom, in DMS was their conve
rsion of ethyl methyl sulfide to ethanethiol. HCHO transiently accumul
ated during the aerobic use of DMS by T. thioparus but not with Thioba
cillus strain ASN-1. Catalase levels in cells grown aerobically on DMS
were about 100-fold lower in Thiobacillus strain ASN-1 than in T. thi
oparus T5, suggesting the absence of H2O2 formation during DMS catabol
ism. Also, aerobic growth of T. thioparus T5 on DMS was blocked by the
catalase inhibitor 3-amino-1,2,4-triazole whereas that of Thiobacillu
s strain ASN-1 was not. Methyl butyl ether, but not CHCl3, blocked DMS
catabolism by T. thioparus T5, presumably by inhibiting DMS monooxyge
nase and perhaps methanethiol oxidase. In contrast, DMS metabolism by
Thiobacillus strain ASN-1 was unaffected by methyl butyl ether but inh
ibited by CHCl3. DMS catabolism by Thiobacillus strain ASN-1 probably
involves methyl transfer to a cobalamin carrier and subsequent oxidati
on as folate-bound intermediates.