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. 2021 Apr 27;12:667343. doi: 10.3389/fimmu.2021.667343

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Copyright © 2021 Sen and Imlay

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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PerR activation. PerR is a dimeric DNA-binding protein, and it binds two metal ions per monomer. The first ion is a structural Zn²⁺ that is necessary for dimerization and structural integrity. The second metal ion enables DNA binding, and can either be Fe²⁺ or Mn²⁺. Only PerR bound to Fe²⁺ is responsive to H₂O₂. The oxidation of Fe²⁺ by H₂O₂ generates a localized hydroxyl/ferryl radical, which irreversibly oxidizes either of two His ligands (H37 or H91) to form 2-oxo-histidine. Metal binding is blocked, PerR dissociates from promoter sites, and the regulon is induced.