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. 2019 Feb 18;10:166. doi: 10.3389/fpls.2019.00166

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Copyright © 2019 Dumont and Rivoal.

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) and the copyright owner(s) 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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Different redox modifications of protein Cys thiols and their reversibility. Protein thiol oxidation can lead to a variety of redox modifications. The scheme presents the relations between the different redox modifications and the reversibility of these modifications. Sulfonic acid (–SO₃H) formation is considered to be irreversible as well as sulfinic acid (–SO₂H) except in the case of certain peroxiredoxins which sulfinic acid Cys residue can be reduced by sulfiredoxin using and ATP-dependent mechanism. See text for details. ROS, reactive oxygen species; RNS, reactive nitrogen species; H₂S, hydrogen sulfide; GSSG, oxidized glutathione; GSH, reduced glutathione; ASC, ascorbate; GRX, glutaredoxin; TRX, thioredoxin; SRX, sulfiredoxin; R-SH, reduced thiol; R-S^-, thiolate anion; R-SOH, sulfenic acid; R-SNO, protein S-nitrosylation; R-SSG, protein S-glutathionylation Cys; R-SSH, protein S-sulfhydration; R-SS-R, disulfide bond.