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

Department of Clinical Biochemistry

4 Citations (Scopus)

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 : PPB / Société française de physiologie végétale
Volume	90
Pages (from-to)	58-63
Number of pages	6
DOIs	https://doi.org/10.1016/j.plaphy.2015.03.003
Publication status	Published - May 2015

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A redox-dependent dimerization switch regulates activity and tolerance for reactive oxygen species of barley seed glutathione peroxidase. / Navrot, Nicolas; Skjoldager, Nicklas; Bunkenborg, Jakob et al.
In: Plant physiology and biochemistry : PPB / Société française de physiologie végétale, Vol. 90, 05.2015, p. 58-63.

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

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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.",

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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 - 2015/5

Y1 - 2015/5

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.

U2 - 10.1016/j.plaphy.2015.03.003

DO - 10.1016/j.plaphy.2015.03.003

M3 - Journal article

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SN - 1873-2690

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SP - 58

EP - 63

JO - Plant physiology and biochemistry : PPB / Société française de physiologie végétale

JF - Plant physiology and biochemistry : PPB / Société française de physiologie végétale

ER -

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

Abstract

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