ArticleScientific reports2016
Catalytic Thr or Ser Residue Modulates Structural Switches in 2-Cys Peroxiredoxin by Distinct Mechanisms.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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Who cites it
24 citing papers in PubMed, 62 citations in OpenAlex.
- Hetero-oligomerization drives structural plasticity of eukaryotic peroxiredoxins.Nature chemical biology · 2026Article
- Is uric acid a true antioxidant? Identification of uric acid oxidation products and their biological effects.Redox report : communications in free radical research · 2025Review
- Linoleic Hydroperoxides Are Potent Hyperoxidative Agents of Sensitive and Robust Typical 2-Cys Peroxiredoxins.Antioxidants (Basel, Switzerland) · 2025Article
- Cold-adapted characteristics and gene knockout of alkyl hydroperoxide reductase subunit C in Antarctic Psychrobacter sp. ANT206.World journal of microbiology & biotechnology · 2024Article
- Disulfide-Bond-Induced Structural Frustration and Dynamic Disorder in a Peroxiredoxin from MAS NMR.Journal of the American Chemical Society · 2023Article
- Article
- Basis for using thioredoxin as an electron donor by Schizosaccharomyces pombe Gpx1 and Tpx1.AMB Express · 2022Article
- Relevance of peroxiredoxins in pathogenic microorganisms.Applied microbiology and biotechnology · 2021Review
- Effects of Serine or Threonine in the Active Site of Typical 2-Cys Prx on Hyperoxidation Susceptibility and on Chaperone Activity.Antioxidants (Basel, Switzerland) · 2021Article
- Functional and structural evaluation of the antileukaemic enzyme L-asparaginase II expressed at low temperature by different Escherichia coli strains.Biotechnology letters · 2020Article
- Real-time monitoring of peroxiredoxin oligomerization dynamics in living cells.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Thiol Peroxidases as Major Regulators of Intracellular Levels of Peroxynitrite in LiveAntioxidants (Basel, Switzerland) · 2020Article
- The Peroxidatic Thiol of Peroxiredoxin 1 is Nitrosated by Nitrosoglutathione but Coordinates to the Dinitrosyl Iron Complex of Glutathione.Antioxidants (Basel, Switzerland) · 2020Article
- Dynamics of a Key Conformational Transition in the Mechanism of Peroxiredoxin Sulfinylation.ACS catalysis · 2020Article
- The Human PathogenFrontiers in cellular and infection microbiology · 2020Article
- The bicarbonate/carbon dioxide pair increases hydrogen peroxide-mediated hyperoxidation of human peroxiredoxin 1.The Journal of biological chemistry · 2019Article
- Aromatic Residues at the Dimer-Dimer Interface in the Peroxiredoxin Tsa1 Facilitate Decamer Formation and Biological Function.Chemical research in toxicology · 2019Article
- Piecing Together How Peroxiredoxins Maintain Genomic Stability.Antioxidants (Basel, Switzerland) · 2018Review
- Analyses of the three 1-Cys Peroxiredoxins from Aspergillus fumigatus reveal that cytosolic Prx1 is central to HScientific reports · 2018Article
- Experimentally Dissecting the Origins of Peroxiredoxin Catalysis.Antioxidants & redox signaling · 2018Article
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Typical 2-Cys Peroxiredoxins (2-Cys Prxs) reduce hydroperoxides with extraordinary rates due to an active site composed of a catalytic triad, containing a peroxidatic cysteine (CP), an Arg, and a Thr (or Ser). 2-Cys Prx are involved in processes such as cancer; neurodegeneration and host-pathogen interactions. During catalysis, 2-Cys Prxs switch between decamers and dimers. Analysis of 2-Cys Prx structures in the fully folded (but not locally unfolded) form revealed a highly conserved, non-conventional hydrogen bond (CH-π) between the catalytic triad Thr of a dimer with an aromatic residue of an adjacent dimer. In contrast, structures of 2-Cys Prxs with a Ser in place of the Thr do not display this CH-π bond. Chromatographic and structural data indicate that the Thr (but not Ser) destabilizes the decamer structure in the oxidized state probably through steric hindrance. As a general trend, mutations in a yeast 2-Cys Prx (Tsa1) favoring the dimeric state also displayed a decreased catalytic activity. Remarkably, yeast naturally contains Thr-Ser variants (Tsa1 and Tsa2, respectively) with distinct oligomeric stabilities in their disulfide states.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.