A redox-dependent dimerization switch regulates activity and tolerance for reactive oxygen species of barley seed glutathione peroxidase

Nicolas Navrot, Nicklas Skjoldager, Jakob Bunkenborg, Birte Svensson, Per Hägglund

    Research output: Contribution to journalJournal articleResearchpeer-review

    Abstract

    Monomeric and dimeric forms of recombinant barley (Hordeum vulgare subsp. vulgare) glutathione peroxidase 2 (HvGpx2) are demonstrated to display distinctly different functional properties in vitro. Monomeric HvGpx2 thus has five fold higher catalytic efficiency than the dimer towards tert-butyl hydroperoxide, but is more sensitive to inactivation by hydrogen peroxide. Treatment of the monomer with hydrogen peroxide results in dimer formation. This observed new behavior of a plant glutathione peroxidase suggests a mechanism involving a switch from a highly catalytically competent monomer to a less active, but more oxidation-resistant dimer. 
    Original languageEnglish
    JournalPlant Physiology and Biochemistry
    Volume90
    Pages (from-to)58-63
    Number of pages6
    ISSN0981-9428
    DOIs
    Publication statusPublished - 2015

    Keywords

    • Glutathione peroxidase
    • Thioredoxin
    • Antioxidant
    • Hydrogen peroxide
    • Alkyl peroxide
    • Oligomerization

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