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Rhodanese as a thioredoxin oxidase.

D L Nandi1, P M Horowitz, J Westley

  • 1Department of Biochemistry and Molecular Biology, The University of Chicago, IL 60637, USA.

The International Journal of Biochemistry & Cell Biology
|April 13, 2000
PubMed
Summary
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Two bovine liver mitochondrial rhodanese isoforms exhibit distinct catalytic activities. One isoform oxidizes reduced thioredoxin, suggesting a role in detoxifying oxygen free radicals within mitochondria.

Area of Science:

  • Biochemistry
  • Mitochondrial Biology
  • Enzymology

Background:

  • Rhodanese (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1) is a key mitochondrial enzyme.
  • Two common isoforms of bovine liver mitochondrial rhodanese exist.
  • Understanding rhodanese isoform function is crucial for mitochondrial redox homeostasis.

Purpose of the Study:

  • To investigate the catalytic differences between bovine liver mitochondrial rhodanese isoforms.
  • To elucidate the mechanism of thioredoxin interaction with rhodanese isoforms.
  • To explore the potential role of rhodanese in reactive oxygen species detoxification.

Main Methods:

  • Enzyme kinetics assays comparing rhodanese isoforms.
  • Characterization of substrate specificity with reduced thioredoxin.

Related Experiment Videos

  • Analysis of rhodanese activity in the presence of reactive oxygen species.
  • Main Results:

    • Both rhodanese isoforms accept sulfur from thiosulfate and transfer it to reduced thioredoxin.
    • Only the less negative rhodanese isoform, similar to recombinant mammalian rhodanese, directly oxidizes reduced thioredoxin.
    • This oxidation is linked to reactive oxygen species and involves sulfenic acid intermediates.

    Conclusions:

    • A significant catalytic divergence exists between bovine liver mitochondrial rhodanese isoforms.
    • One isoform possesses thioredoxin oxidase activity, potentially involving reactive oxygen species.
    • This suggests a specific role for this rhodanese isoform in mitigating intramitochondrial oxidative stress.