ArticleStructure (London, England : 1993)2016
Peroxiredoxin Catalysis at Atomic Resolution.
Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 47 citations in OpenAlex.
- Profiling the secretome: maternal obesity impacts redox and adipogenic signaling during neonatal mesenchymal stem cell adipogenesis.Stem cells (Dayton, Ohio) · 2026Article
- Modelling the Decamerisation Cycle of PRDX1 and the Inhibition-like Effect on Its Peroxidase Activity.Antioxidants (Basel, Switzerland) · 2023Article
- Native state fluctuations in a peroxiredoxin active site match motions needed for catalysis.Structure (London, England : 1993) · 2022Article
- A Bacterial Inflammation Sensor Regulates c-di-GMP Signaling, Adhesion, and Biofilm Formation.mBio · 2021Article
- Additive CHARMM36 Force Field for Nonstandard Amino Acids.Journal of chemical theory and computation · 2021Article
- Peroxiredoxins wear many hats: Factors that fashion their peroxide sensing personalities.Redox biology · 2021Review
- Dynamics of a Key Conformational Transition in the Mechanism of Peroxiredoxin Sulfinylation.ACS catalysis · 2020Article
- Structural preferences of cysteine sulfinic acid: The sulfinate engages in multiple local interactions with the peptide backbone.Free radical biology & medicine · 2020Article
- Article
- Redox Signaling by Reactive Electrophiles and Oxidants.Chemical reviews · 2018Review
- Novel hyperoxidation resistance motifs in 2-Cys peroxiredoxins.The Journal of biological chemistry · 2018Article
- Differential Kinetics of Two-Cysteine Peroxiredoxin Disulfide Formation Reveal a Novel Model for Peroxide Sensing.Biochemistry · 2018Article
- Experimentally Dissecting the Origins of Peroxiredoxin Catalysis.Antioxidants & redox signaling · 2018Article
- Systematic and Quantitative Assessment of Hydrogen Peroxide Reactivity With Cysteines Across Human Proteomes.Molecular & cellular proteomics : MCP · 2017Article
- Detection of Reaction Intermediates in MgMethods in enzymology · 2017Article
- Modifying the resolving cysteine affects the structure and hydrogen peroxide reactivity of peroxiredoxin 2.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Peroxiredoxins (Prxs) are ubiquitous cysteine-based peroxidases that guard cells against oxidative damage, are virulence factors for pathogens, and are involved in eukaryotic redox regulatory pathways. We have analyzed catalytically active crystals to capture atomic resolution snapshots of a PrxQ subfamily enzyme (from Xanthomonas campestris) proceeding through thiolate, sulfenate, and sulfinate species. These analyses provide structures of unprecedented accuracy for seeding theoretical studies, and reveal conformational intermediates giving insight into the reaction pathway. Based on a highly non-standard geometry seen for the sulfenate intermediate, we infer that the sulfenate formation itself can strongly promote local unfolding of the active site to enhance productive catalysis. Further, these structures reveal that preventing local unfolding, in this case via crystal contacts, results in facile hyperoxidative inactivation even for Prxs normally resistant to such inactivation. This supports previous proposals that conformation-specific inhibitors may be useful for achieving selective inhibition of Prxs that are drug targets.
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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.