Rhodanese as a thioredoxin oxidase

Dhirendra L. Nandi, Paul M. Horowitz, John Westley

Resultado de la investigación: Articlerevisión exhaustiva

92 Citas (Scopus)


A major catalytic difference between the two most common isoforms of bovine liver mitochondrial rhodanese (thiosulfate: cyanide sulfurtransferase, EC has been observed. Both isoforms were shown to be capable of using reduced thioredoxin as a sulfur-acceptor substrate. However, only the less negative form in common with the recombinant mammalian rhodanese expressed in E. coli, can also catalyze the direct oxidation of reduced thioredoxin evidently by reactive oxygen species. These activities are understood in terms of the established persulfide structure (R-S-SH) of the covalently substituted rhodanese in the sulfurtransferase reaction and an analogous sulfenic acid structure (R-S-OH) when the enzyme acts as a thioredoxin oxidase. The observations suggest a role for one rhodanese isoform in the detoxication of intramitochondrial oxygen free radicals. Copyright (C) 2000.

Idioma originalEnglish (US)
Páginas (desde-hasta)465-473
Número de páginas9
PublicaciónInternational Journal of Biochemistry and Cell Biology
EstadoPublished - abr 2000
Publicado de forma externa

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology


Profundice en los temas de investigación de 'Rhodanese as a thioredoxin oxidase'. En conjunto forman una huella única.

Citar esto