Journal article
A redox-dependent dimerization switch regulates activity and tolerance for reactive oxygen species of barley seed glutathione peroxidase
In
Plant Physiology and Biochemistry
—
2015, Volume 90, pp. 58-63
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.
| Language: | English |
|---|---|
| Year: | 2015 |
| Pages: | 58-63 |
| ISSN: | 18732690 and 09819428 |
| Types: | Journal article |
| DOI: | 10.1016/j.plaphy.2015.03.003 |
| ORCIDs: | Svensson, Birte |
