| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2014991 | Plant Physiology and Biochemistry | 2015 | 6 Pages |
•Recombinant HvGpx2 is produced in monomeric and dimeric forms.•Monomeric HvGpx2 has higher catalytic efficiency compared to the dimer.•Dimeric HvGpx2 is more resistant to inactivation compared to the monomer.•HvGpx2 dimerizes upon treatment with hydrogen peroxide.
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.
