RT Journal Article SR Electronic(1) A1 Rohwerder, Thore A1 Sand, WolfgangYR 2003 T1 The sulfane sulfur of persulfides is the actual substrate of the sulfur-oxidizing enzymes from Acidithiobacillus and Acidiphilium spp. JF Microbiology, VO 149 IS 7 SP 1699 OP 1710 DO https://doi.org/10.1099/mic.0.26212-0 PB Microbiology Society, SN 1465-2080, AB To identify the actual substrate of the glutathione-dependent sulfur dioxygenase (EC 1.13.11.18) elemental sulfur oxidation of the meso-acidophilic Acidithiobacillus thiooxidans strains DSM 504 and K6, Acidithiobacillus ferrooxidans strain R1 and Acidiphilium acidophilum DSM 700 was analysed. Extraordinarily high specific sulfur dioxygenase activities up to 460 nmol min−1 (mg protein)−1 were found in crude extracts. All cell-free systems oxidized elemental sulfur only via glutathione persulfide (GSSH), a non-enzymic reaction product from glutathione (GSH) and elemental sulfur. Thus, GSH plays a catalytic role in elemental sulfur activation, but is not consumed during enzymic sulfane sulfur oxidation. Sulfite is the first product of sulfur dioxygenase activity; it further reacted non-enzymically to sulfate, thiosulfate or glutathione S-sulfonate (). Free sulfide was not oxidized by the sulfur dioxygenase. Persulfide as sulfur donor could not be replaced by other sulfane-sulfur-containing compounds (thiosulfate, polythionates, bisorganyl-polysulfanes or monoarylthiosulfonates). The oxidation of H2S by the dioxygenase required GSSG, i.e. the disulfide of GSH, which reacted non-enzymically with sulfide to give GSSH prior to enzymic oxidation. On the basis of these results and previous findings a biochemical model for elemental sulfur and sulfide oxidation in Acidithiobacillus and Acidiphilium spp. is proposed., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.26212-0