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

Research output: Contribution to journalJournal articleResearchpeer-review

Monomeric and dimeric forms of recombinant barley (Hordeum vulgare subsp. vulgare) glutathione peroxidase 2 (HvGpx2) are demonstrated to display distinctly different functional properties invitro. 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 - 1 May 2015

    Research areas

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

ID: 240157696