ArticleBiochemistry2013
The sensitive balance between the fully folded and locally unfolded conformations of a model peroxiredoxin.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 57 citations in OpenAlex.
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- Cold-adapted characteristics and gene knockout of alkyl hydroperoxide reductase subunit C in Antarctic Psychrobacter sp. ANT206.World journal of microbiology & biotechnology · 2024Article
- Regulation of NADP-Malic Enzyme Activity in Maize (Plants (Basel, Switzerland) · 2023Article
- Article
- Native state fluctuations in a peroxiredoxin active site match motions needed for catalysis.Structure (London, England : 1993) · 2022Article
- Peroxiredoxins wear many hats: Factors that fashion their peroxide sensing personalities.Redox biology · 2021Review
- Real-time monitoring of peroxiredoxin oligomerization dynamics in living cells.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Predicting Reactive Cysteines with Implicit-Solvent-Based Continuous Constant pH Molecular Dynamics in Amber.Journal of chemical theory and computation · 2020Article
- Dynamics of a Key Conformational Transition in the Mechanism of Peroxiredoxin Sulfinylation.ACS catalysis · 2020Article
- Helicobacter pylori senses bleach (HOCl) as a chemoattractant using a cytosolic chemoreceptor.PLoS biology · 2019Article
- Global Implications of Local Unfolding Phenomena, Probed by Cysteine Reactivity in Human Frataxin.Scientific reports · 2019Article
- Structural snapshots of OxyR reveal the peroxidatic mechanism of HProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Piecing Together How Peroxiredoxins Maintain Genomic Stability.Antioxidants (Basel, Switzerland) · 2018Review
- Monitoring the action of redox-directed cancer therapeutics using a human peroxiredoxin-2-based probe.Nature communications · 2018Article
- 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
- Urate hydroperoxide oxidizes human peroxiredoxin 1 and peroxiredoxin 2.The Journal of biological chemistry · 2017Article
- Evolution and function of the Mycoplasma hyopneumoniae peroxiredoxin, a 2-Cys-like enzyme with a single Cys residue.Molecular genetics and genomics : MGG · 2017Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
To reduce peroxides, peroxiredoxins (Prxs) require a key "peroxidatic" Cys that, in a substrate-ready fully folded (FF) conformation, is oxidized to sulfenic acid and then, after a local unfolding (LU) of the active site, forms a disulfide bond with a second "resolving" Cys. For Salmonella typhimurium alkyl hydroperoxide reductase C (StAhpC) and some other Prxs, the FF structure is only known for a peroxidatic Cys→Ser variant, which may not accurately represent the wild-type enzyme. Here, we obtain the structure of authentic reduced wild-type StAhpC by dithiothreitol treatment of disulfide form crystals that fortuitously accommodate both the LU and FF conformations. The unique environment of one molecule in the crystal reveals a thermodynamic linkage between the folding of the active site loop and C-terminal regions, and comparisons with the Ser variant show structural and mobility differences from which we infer that the Cys→Ser mutation stabilizes the FF active site. A structure for the C165A variant (a resolving Cys to Ala mutant) in the same crystal form reveals that this mutation destabilizes the folding of the C-terminal region. These structures prove that subtle modifications to Prx structures can substantially influence enzymatic properties. We also present a simple thermodynamic framework for understanding the various mixtures of FF and LU conformations seen in these structures. On the basis of this framework, we rationalize how physiologically relevant regulatory post-translational modifications may modulate activity, and we propose a nonconventional strategy for designing selective Prx inhibitors.
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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.