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. 2017 Jan 10;6(2):139–153. doi: 10.3892/mco.2017.1129

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Copyright: © Nicolussi et al.

This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.

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Figure 4. — Catalytic mechanism of typical 2-Cys PRDXa. (A) PRDXs switch from an FF conformation, in which C_p reacts with the peroxide, to an LU conformation, in which the C_p is exposed and forms a disulfide bridge with the C_r residue. The thiol groups are converted into sulfenic acid (−S-OH) and form disulfide bonds with other thiol groups (−SS-) (oxidized status-LU conformation). At high peroxide concentrations, the sulfenic acid intermediate is overoxidized to sulfinic acid (−SOOH) or even sulfonic acid (−SOOOH), causing the inactivation of the enzyme (hyperoxidized status). (B) Stereo-view of the interpolated structural changes shown in rainbow colors between the FF (blue) and LU (red) conformations for a representative of Prx1 subfamily (upper) and Prx5 subfamily (lower). PRDX, peroxiredoxin; Srx1 sulfiredoxin 1, Trx, thioredoxin; TrxR, thioredoxin reductase; FF, fully folded; LU, locally unfolded.