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

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Title: A redox-dependent dimerization switch regulates activity and tolerance for reactive oxygen species of barley seed glutathione peroxidase
Authors: Navrot, Nicolas, Skjoldager, Nicklas, Bunkenborg, Jakob, Svensson, Birte, Hägglund, Per
Source: Navrot, N, Skjoldager, N, Bunkenborg, J, Svensson, B & Hägglund, P 2015, ' A redox-dependent dimerization switch regulates activity and tolerance for reactive oxygen species of barley seed glutathione peroxidase ', Plant Physiology and Biochemistry, vol. 90, pp. 58-63 . https://doi.org/10.1016/j.plaphy.2015.03.003
Publisher Information: Elsevier BV, 2015.
Publication Year: 2015
Subject Terms: 0301 basic medicine, Physiological, 03 medical and health sciences, tert-Butylhydroperoxide, Reactive Oxygen Species/metabolism, Oligomerization, Alkyl peroxide, Adaptation, Hordeum/enzymology, Thioredoxin, Hydrogen Peroxide/metabolism, Seeds/metabolism, Glutathione Peroxidase, 0303 health sciences, Glutathione Peroxidase/metabolism, Peroxidases/metabolism, Hordeum, Hydrogen Peroxide, Peroxiredoxins, Hydrogen peroxide, Adaptation, Physiological, Glutathione, Glutathione/metabolism, 3. Good health, Oxidative Stress, Peroxidases, Seeds, Glutathione peroxidase, Peroxiredoxins/metabolism, Antioxidant, Reactive Oxygen Species, tert-Butylhydroperoxide/metabolism, Dimerization, Oxidation-Reduction
Description: 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.
Document Type: Article
Language: English
ISSN: 0981-9428
DOI: 10.1016/j.plaphy.2015.03.003
Access URL: https://pubmed.ncbi.nlm.nih.gov/25796076
https://orbit.dtu.dk/en/publications/a-redoxdependent-dimerization-switch-regulates-activity-and-tolerance-for-reactive-oxygen-species-of-barley-seed-glutathione-peroxidase(c53e98ee-c4a5-427b-8c03-79be1755cb66).html
https://europepmc.org/abstract/MED/25796076
http://europepmc.org/abstract/MED/25796076
http://orbit.dtu.dk/en/publications/a-redoxdependent-dimerization-switch-regulates-activity-and-tolerance-for-reactive-oxygen-species-of-barley-seed-glutathione-peroxidase(c53e98ee-c4a5-427b-8c03-79be1755cb66).html
https://www.sciencedirect.com/science/article/pii/S0981942815000571
https://pubag.nal.usda.gov/catalog/5433255
https://portal.findresearcher.sdu.dk/da/publications/095818b9-7381-4e89-8047-5ed7e0527ba8
https://portal.findresearcher.sdu.dk/da/publications/095818b9-7381-4e89-8047-5ed7e0527ba8
https://doi.org/10.1016/j.plaphy.2015.03.003
Rights: Elsevier TDM
Accession Number: edsair.doi.dedup.....4627dbd9d83d899d2caab86e5086074b
Database: OpenAIRE
Description
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.
ISSN:09819428
DOI:10.1016/j.plaphy.2015.03.003