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

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

A redox-dependent dimerization switch regulates activity and tolerance for reactive oxygen species of barley seed glutathione peroxidase. / Navrot, Nicolas; Skjoldager, Nicklas; Bunkenborg, Jakob; Svensson, Birte; Hägglund, Per.

In: Plant Physiology and Biochemistry, Vol. 90, 2015, p. 58-63.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

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

APA

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, 90, 58-63. https://doi.org/10.1016/j.plaphy.2015.03.003

Vancouver

Navrot N, Skjoldager N, Bunkenborg J, Svensson B, Hägglund P. A redox-dependent dimerization switch regulates activity and tolerance for reactive oxygen species of barley seed glutathione peroxidase. Plant Physiology and Biochemistry. 2015;90:58-63. https://doi.org/10.1016/j.plaphy.2015.03.003

Author

Navrot, Nicolas ; Skjoldager, Nicklas ; Bunkenborg, Jakob ; Svensson, Birte ; Hägglund, Per. / A redox-dependent dimerization switch regulates activity and tolerance for reactive oxygen species of barley seed glutathione peroxidase. In: Plant Physiology and Biochemistry. 2015 ; Vol. 90. pp. 58-63.

Bibtex

@article{ad6536eda7234f6c8299015063102a68,
title = "A redox-dependent dimerization switch regulates activity and tolerance for reactive oxygen species of barley seed glutathione peroxidase",
abstract = "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.",
keywords = "Alkyl peroxide, Antioxidant, Glutathione peroxidase, Hydrogen peroxide, Oligomerization, Thioredoxin",
author = "Nicolas Navrot and Nicklas Skjoldager and Jakob Bunkenborg and Birte Svensson and Per H{\"a}gglund",
year = "2015",
doi = "10.1016/j.plaphy.2015.03.003",
language = "English",
volume = "90",
pages = "58--63",
journal = "Plant Physiology and Biochemistry",
issn = "0981-9428",
publisher = "Elsevier Masson",

}

RIS

TY - JOUR

T1 - A redox-dependent dimerization switch regulates activity and tolerance for reactive oxygen species of barley seed glutathione peroxidase

AU - Navrot, Nicolas

AU - Skjoldager, Nicklas

AU - Bunkenborg, Jakob

AU - Svensson, Birte

AU - Hägglund, Per

PY - 2015

Y1 - 2015

N2 - 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.

AB - 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.

KW - Alkyl peroxide

KW - Antioxidant

KW - Glutathione peroxidase

KW - Hydrogen peroxide

KW - Oligomerization

KW - Thioredoxin

U2 - 10.1016/j.plaphy.2015.03.003

DO - 10.1016/j.plaphy.2015.03.003

M3 - Journal article

C2 - 25796076

AN - SCOPUS:84924975473

VL - 90

SP - 58

EP - 63

JO - Plant Physiology and Biochemistry

JF - Plant Physiology and Biochemistry

SN - 0981-9428

ER -

ID: 240157696