Differentiation of the roles of sulfide oxidase and rhodanese in the detoxification of sulfide by the colonic mucosa

Kirk Wilson, Mitchell Mudra, Julie Furne, Michael Levitt

Research output: Contribution to journalArticlepeer-review

30 Scopus citations


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 languageEnglish (US)
Pages (from-to)277-283
Number of pages7
JournalDigestive Diseases and Sciences
Issue number1
StatePublished - Jan 2008

Bibliographical note

Funding 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
  • Sulfurtransferase
  • Thiosulfate


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