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

Nicolas Navrot; Nicklas Skjoldager; Jakob Bunkenborg; Birte Svensson; Per Hägglund

doi:10.1016/j.plaphy.2015.03.003

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

Nicolas Navrot, Nicklas Skjoldager, Jakob Bunkenborg, Birte Svensson, Per Hägglund

University of Southern Denmark

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

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.

Original language	English
Journal	Plant Physiology and Biochemistry
Volume	90
Pages (from-to)	58-63
Number of pages	6
ISSN	0981-9428
DOIs	https://doi.org/10.1016/j.plaphy.2015.03.003
Publication status	Published - 2015

Keywords

Glutathione peroxidase
Thioredoxin
Antioxidant
Hydrogen peroxide
Alkyl peroxide
Oligomerization

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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 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. ",

keywords = "Glutathione peroxidase, Thioredoxin, Antioxidant, Hydrogen peroxide, Alkyl peroxide, Oligomerization",

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",

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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 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.

AB - 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.

KW - Glutathione peroxidase

KW - Thioredoxin

KW - Antioxidant

KW - Hydrogen peroxide

KW - Alkyl peroxide

KW - Oligomerization

U2 - 10.1016/j.plaphy.2015.03.003

DO - 10.1016/j.plaphy.2015.03.003

M3 - Journal article

C2 - 25796076

SN - 0981-9428

VL - 90

SP - 58

EP - 63

JO - Plant Physiology and Biochemistry

JF - Plant Physiology and Biochemistry

ER -

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

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Keywords

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