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Related Experiment Videos

Thioredoxin-dependent peroxide reductase from yeast

H Z Chae1, S J Chung, S G Rhee

  • 1Laboratory of Biochemistry, NHLBI, National Institutes of Health, Bethesda, Maryland 20892.

The Journal of Biological Chemistry
|November 4, 1994
PubMed
Summary
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A newly identified 25-kDa antioxidant enzyme, thioredoxin peroxidase (TPx), functions as a peroxidase. It utilizes thioredoxin, thioredoxin reductase, and NADPH to reduce harmful reactive oxygen and sulfur species.

Area of Science:

  • Biochemistry
  • Enzymology
  • Oxidative Stress Research

Background:

  • A 25-kDa antioxidant enzyme was previously identified but its specific function and reducing equivalents were unknown.
  • Reactive oxygen and sulfur species pose significant threats through oxidative damage.

Purpose of the Study:

  • To elucidate the specific oxidant neutralized by the 25-kDa enzyme.
  • To identify the physiological source of reducing equivalents for this antioxidant enzyme.
  • To characterize the novel thioredoxin-dependent peroxidase activity.

Main Methods:

  • Enzyme activity assays using hydrogen peroxide and alkyl hydroperoxides.
  • Identification of hydrogen donors including thioredoxin, thioredoxin reductase, and NADPH.
  • Site-directed mutagenesis of cysteine residues (Cys47 and Cys170) within the enzyme.

Related Experiment Videos

  • Characterization of disulfide reduction by thioredoxin and other thiols.
  • Cloning and sequencing of the Saccharomyces cerevisiae thioredoxin reductase gene.

    • Main Results:

    • The 25-kDa enzyme is a peroxidase reducing hydrogen peroxide and alkyl hydroperoxides.
    • Thioredoxin serves as the immediate hydrogen donor, leading to its naming as thioredoxin peroxidase (TPx).
    • Cysteine 47 is the oxidation site, forming an intermolecular disulfide with Cysteine 170, essential for activity.
    • Mutant enzymes lacking Cys47 or Cys170 are inactive.
    • TPx disulfide is specifically reduced by thioredoxin.
    • The Saccharomyces cerevisiae thioredoxin reductase shares 51% sequence identity with the E. coli enzyme.

    Conclusions:

    • Thioredoxin peroxidase (TPx) is a novel enzyme crucial for combating oxidative stress.
    • TPx utilizes a unique thioredoxin-dependent mechanism for peroxide reduction.
    • The identified cysteine residues and their disulfide bond formation are critical for TPx function.
    • The findings provide insights into cellular antioxidant defense systems.