ArticleThe Journal of biological chemistry2013
Multilevel regulation of 2-Cys peroxiredoxin reaction cycle by S-nitrosylation.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 63 citations in OpenAlex.
- Context‑dependent targeting of thioredoxin reductase 1 in cancer: a mechanistic review.Magyar onkologia · 2026Review
- Hetero-oligomerization drives structural plasticity of eukaryotic peroxiredoxins.Nature chemical biology · 2026Article
- Moonlighting Functions of Mammalian Peroxiredoxins in Cellular Signaling.Antioxidants (Basel, Switzerland) · 2026Review
- Peroxiredoxin 2: An Important Element of the Antioxidant Defense of the Erythrocyte.Antioxidants (Basel, Switzerland) · 2023Review
- Celastrol suppresses colorectal cancer via covalent targeting peroxiredoxin 1.Signal transduction and targeted therapy · 2023Article
- Thioredoxins: Emerging Players in the Regulation of Protein S-Nitrosation in Plants.Plants (Basel, Switzerland) · 2020Review
- Oxidants, Antioxidants and Thiol Redox Switches in the Control of Regulated Cell Death Pathways.Antioxidants (Basel, Switzerland) · 2020Review
- The Peroxidatic Thiol of Peroxiredoxin 1 is Nitrosated by Nitrosoglutathione but Coordinates to the Dinitrosyl Iron Complex of Glutathione.Antioxidants (Basel, Switzerland) · 2020Article
- Opposing effects of polysulfides and thioredoxin on apoptosis through caspase persulfidation.The Journal of biological chemistry · 2020Article
- Redox Post-translational Modifications of Protein Thiols in Brain Aging and Neurodegenerative Conditions-Focus on S-Nitrosation.Frontiers in aging neuroscience · 2020Review
- The bicarbonate/carbon dioxide pair increases hydrogen peroxide-mediated hyperoxidation of human peroxiredoxin 1.The Journal of biological chemistry · 2019Article
- Unraveling the effects of peroxiredoxin 2 nitration; role of C-terminal tyrosine 193.Free radical biology & medicine · 2019Article
- Differential parameters between cytosolic 2-Cys peroxiredoxins, PRDX1 and PRDX2.Protein science : a publication of the Protein Society · 2019Article
- S-Nitrosylation of α1-Antitrypsin Triggers Macrophages Toward Inflammatory Phenotype and Enhances Intra-Cellular Bacteria Elimination.Frontiers in immunology · 2019Article
- Peroxiredoxins in Cancer and Response to Radiation Therapies.Antioxidants (Basel, Switzerland) · 2019Review
- Nitric Oxide Engages an Anti-inflammatory Feedback Loop Mediated by Peroxiredoxin 5 in Phagocytes.Cell reports · 2018Article
- Cellular Timekeeping: It's Redox o'Clock.Cold Spring Harbor perspectives in biology · 2018Review
- Peroxiredoxins and Redox Signaling in Plants.Antioxidants & redox signaling · 2018Review
- Crystal structure of peroxiredoxin 3 fromIUCrJ · 2018Article
- S-Nitrosylation Regulates Cell Survival and Death in the Central Nervous System.Neurochemical research · 2018Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
S-nitrosothiols (SNOs), formed by nitric oxide (NO)-mediated S-nitrosylation, and hydrogen peroxide (H2O2), a prominent reactive oxygen species, are implicated in diverse physiological and pathological processes. Recent research has shown that the cellular action and metabolism of SNOs and H2O2 involve overlapping, thiol-based mechanisms, but how these reactive species may affect each other's fate and function is not well understood. In this study we investigated how NO/SNO may affect the redox cycle of mammalian peroxiredoxin-1 (Prx1), a representative of the 2-Cys Prxs, a group of thioredoxin (Trx)-dependent peroxidases. We found that, both in a cell-free system and in cells, NO/SNO donors such as S-nitrosocysteine and S-nitrosoglutathione readily induced the S-nitrosylation of Prx1, causing structural and functional alterations. In particular, nitrosylation promoted disulfide formation involving the pair of catalytic cysteines (Cys-52 and Cys-173) and disrupted the oligomeric structure of Prx1, leading to loss of peroxidase activity. A highly potent inhibition of the peroxidase catalytic reaction by NO/SNO was seen in assays employing the coupled Prx-Trx system. In this setting, S-nitrosocysteine (10 μM) effectively blocked the Trx-mediated regeneration of oxidized Prx1. This effect appeared to be due to both competition between S-nitrosocysteine and Prx1 for the Trx system and direct modulation by S-nitrosocysteine of Trx reductase activity. Our findings that NO/SNO target both Prx and Trx reductase may have implications for understanding the impact of nitrosylation on cellular redox homeostasis.
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