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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10.1016/j.plaphy.2015.03.003

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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",

issn = "0981-9428",

publisher = "Elsevier Masson s.r.l.",

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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 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

Abstract

Keywords

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