Purpose: Identify the roles of sulfide oxidase and rhodanese in sulfide detoxification in rat colonic mucosa. Results: Gel filtration of colonic mucosa and purified bovine rhodanese showed that rhodanese and sulfide oxidizing activities resided in different proteins. In the presence of cyanide, rhodanese shifted the major mucosal metabolite of sulfide from thiosulfate to thiocyanate. The purported ability of purified rhodanese to metabolize sulfide reflects: (a) contamination with a sulfide oxidase, and (b) the spontaneous conversion of sulfide to thiosulfate during storage; rhodanese then catalyzes the conversion of this thiosulfate to thiocyanate. Conclusions: Rhodanese does not metabolize sulfide. The rate-limiting step in sulfide detoxification is oxidation by a sulfide oxidase to thiosulfate. Rhodanese then converts this thiosulfate to thiocyanate, but this reaction does not increase the rate of sulfide detoxification. The recent use of rhodanese activity as a surrogate for the rate that colonic mucosa detoxifies sulfide is inappropriate.
|Original language||English (US)|
|Number of pages||7|
|Journal||Digestive Diseases and Sciences|
|State||Published - Jan 2008|
Bibliographical noteFunding Information:
This work was supported by funds from the Department of Veterans Affairs and the Minnesota Veterans Research Institute and the Eli and Edythe L. Broad Foundation.
- Hydrogen sulfide
- Large intestine