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Related Experiment Videos

Ascorbate peroxidase-thioredoxin interaction.

Eric Gelhaye1, Nicolas Navrot, Isabel K Macdonald

  • 1Unité Mixte de Recherches 1136 INRA UHP (Interaction Arbres Microorganismes), IFR 110 Génomique Ecophysiologie et Ecologie Fonctionnelles, Faculté des Sciences, Nancy Université, BP 239, 54506, Vandoeuvre-lès-Nancy Cedex, France. gelhaye@lcb.uhp-nancy.fr

Photosynthesis Research
|October 13, 2006
PubMed
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Ascorbate peroxidase (APX) is inactivated by reduced thioredoxins and glutathione, suggesting a novel regulatory mechanism. This interaction involves thiol oxidation and impacts APX function.

Area of Science:

  • Plant biochemistry
  • Enzyme kinetics
  • Redox biology

Background:

  • Proteomics data suggest ascorbate peroxidase (APX) interacts with thioredoxins.
  • Understanding this interaction is crucial for plant redox homeostasis.

Purpose of the Study:

  • To investigate the interaction between pea cytosolic APX and poplar thioredoxins h.
  • To elucidate the mechanism of APX inactivation by thioredoxins.

Main Methods:

  • Recombinant enzyme assays
  • Oxygen consumption measurements
  • Visible spectrum analysis
  • Fluorimetry
  • Hydrogen peroxide scavenging assays

Main Results:

Related Experiment Videos

  • Reduced thioredoxins h and glutathione drastically inactivated pea cytosolic APX.
  • APX oxidizes thiols, generating thiyl radicals that lead to oxygen reduction and H2O2 production.
  • APX inactivation involves modification of tryptophan residues, indicating a direct structural impact.

    • Conclusions:

    • Thioredoxin-mediated inactivation of APX represents a novel regulatory pathway in plants.
    • This interaction highlights the complex interplay between thioredoxins, glutathione, and APX in cellular redox control.