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. 2016 Nov 10;7:1669. doi: 10.3389/fpls.2016.01669

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Copyright © 2016 Kovacs, Holzmeister, Wirtz, Geerlof, Fröhlich, Römling, Kuruthukulangarakoola, Linster, Hell, Arnold, Durner and Lindermayr.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Dose-dependent inhibition of GSNOR activity by oxidation in vitro. Measurements of GSNO reducing activity of GSNOR protein. Recombinant GSNOR (1 μg) was incubated with indicated concentrations of H₂O₂ (A), N-ethylmaleimide (B), and peroxynitrite (PN) and H₂O₂ (C). For restoring GSNOR activity, 10 mM DTT was added to the H₂O₂ inhibited enzyme (A). Values are expressed as percentage of the control activity (at 0 mM: 87.5–110.9 μmol NADH min^-1 mg^-1 varied among independent purifications) and represent the mean ± SD calculated from three independent assays. Different letters indicate significant differences (p < 0.05, Anova).