Rhodanese as a thioredoxin oxidase

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

Research output: Contribution to journalArticlepeer-review

90 Scopus citations

Abstract

A major catalytic difference between the two most common isoforms of bovine liver mitochondrial rhodanese (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1) 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.

Original languageEnglish (US)
Pages (from-to)465-473
Number of pages9
JournalInternational Journal of Biochemistry and Cell Biology
Volume32
Issue number4
DOIs
StatePublished - Apr 2000
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology

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