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

Journal: Plant physiology and biochemistry : PPB 2015;90():58-63

PMID: 25796076

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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.

Address: Enzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark, Building 224, DK-2800 Kgs. Lyngby, Denmark.; Center of Experimental BioInformatics, Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230 Odense, Denmark; Department of Clinical Biochemistry, Copenhagen University Hospital Hvidovre, DK-2650 Hvidovre, Denmark.; Enzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark, Building 224, DK-2800 Kgs. Lyngby, Denmark. Electronic address: [email protected].

DOI: 10.1016/j.plaphy.2015.03.003

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MeSH Terms: Adaptation, Physiological, Dimerization, Glutathione, Glutathione Peroxidase, Hordeum, Hydrogen Peroxide, Oxidation-Reduction, Oxidative Stress, Peroxidases, Peroxiredoxins, Reactive Oxygen Species, Seeds, tert-Butylhydroperoxide