ArticleThe Biochemical journal2016
Kinetic analysis of structural influences on the susceptibility of peroxiredoxins 2 and 3 to hyperoxidation.
Article in The Biochemical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 36 citations in OpenAlex.
- Origins of Ultrasensitivity and Complex Signaling Dynamics of Cellular Hydrogen Peroxide and Peroxiredoxin.Antioxidants (Basel, Switzerland) · 2025Article
- The architecture of redox microdomains: Cascading gradients and peroxiredoxins' redox-oligomeric coupling integrate redox signaling and antioxidant protection.Redox biology · 2024Article
- Overoxidation and Oligomerization ofPathogens (Basel, Switzerland) · 2023Article
- Modelling the Decamerisation Cycle of PRDX1 and the Inhibition-like Effect on Its Peroxidase Activity.Antioxidants (Basel, Switzerland) · 2023Article
- Mitochondrial Peroxiredoxin 3 Is Rapidly Oxidized and Hyperoxidized by Fatty Acid Hydroperoxides.Antioxidants (Basel, Switzerland) · 2023Article
- Native state fluctuations in a peroxiredoxin active site match motions needed for catalysis.Structure (London, England : 1993) · 2022Article
- Bioinformatic Analyses of Peroxiredoxins and RF-Prx: A Random Forest-Based Predictor and Classifier for Prxs.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Specificity of Human Sulfiredoxin for Reductant and Peroxiredoxin Oligomeric State.Antioxidants (Basel, Switzerland) · 2021Article
- Hyperoxidation of Peroxiredoxins and Effects on Physiology ofAntioxidants (Basel, Switzerland) · 2021Article
- Unique Cellular and Biochemical Features of Human Mitochondrial Peroxiredoxin 3 Establish the Molecular Basis for Its Specific Reaction with Thiostrepton.Antioxidants (Basel, Switzerland) · 2021Article
- Discovery of Spilanthol Endoperoxide as a Redox Natural Compound Active against Mammalian Prx3 andAntioxidants (Basel, Switzerland) · 2020Article
- A curious case of cysteines in human peroxiredoxin I.Redox biology · 2020Article
- Dynamics of a Key Conformational Transition in the Mechanism of Peroxiredoxin Sulfinylation.ACS catalysis · 2020Article
- Peroxiredoxins and Beyond; Redox Systems Regulating Lung Physiology and Disease.Antioxidants & redox signaling · 2019Review
- Transition to 37°C reveals importance of NADPH in mitigating oxidative stress in stored RBCs.JCI insight · 2019Article
- The Multifaceted Impact of Peroxiredoxins on Aging and Disease.Antioxidants & redox signaling · 2018Review
- Cellular Timekeeping: It's Redox o'Clock.Cold Spring Harbor perspectives in biology · 2018Review
- Mapping the phenotypic repertoire of the cytoplasmic 2-Cys peroxiredoxin - Thioredoxin system. 1. Understanding commonalities and differences among cell types.Redox biology · 2018Article
- Peroxiredoxin Involvement in the Initiation and Progression of Human Cancer.Antioxidants & redox signaling · 2018Review
- Experimentally Dissecting the Origins of Peroxiredoxin Catalysis.Antioxidants & redox signaling · 2018Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Mammalian 2-cysteine peroxiredoxins (Prxs) are susceptible to hyperoxidation by excess H2O2. The cytoplasmic family member Prx2 hyperoxidizes more readily than mitochondrial Prx3 due to slower dimerization of the sulfenic acid (SpOH) intermediate. Four variant amino acids near the C-terminus have been shown to contribute to this difference. We have performed kinetic analysis of the relationship between hyperoxidation and disulfide formation, using whole-protein MS and comparing wild-type (WT) Prx2 and Prx3 with tail-swap mutants in which the four amino acids were reversed. These changes make Prx3 more sensitive and Prx2 less sensitive to hyperoxidation and accounted for ∼70% of the difference between the two proteins. The tail swap mutant of Prx3 was also more susceptible when expressed in the mitochondria of HeLa cells. The hyperoxidized product at lower excesses of H2O2 was a semi-hyperoxidized dimer with one active site disulfide and the other a sulfinic acid. For Prx2, increasing the H2O2 concentration resulted in complete hyperoxidation. In contrast, only approximately half the Prx3 active sites underwent hyperoxidation and, even with high H2O2, the predominant product was the hyperoxidized dimer. Size exclusion chromatography (SEC) showed that the oligomeric forms of all redox states of Prx3 dissociated more readily into dimeric units than their Prx2 counterparts. Notably the species with one disulfide and one hyperoxidized active site was decameric for Prx2 and dimeric for Prx3. Reduction and re-oxidation of the hyperoxidized dimer of Prx3 produced hyperoxidized monomers, implying dissociation and rearrangement of the subunits of the functional homodimer.
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