ArticleRedox biology2020
A dual attack on the peroxide bond. The common principle of peroxidatic cysteine or selenocysteine residues.
Article in Redox biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 30 citations in OpenAlex.
- 50 Years of Organoselenium Chemistry, Biochemistry and Reactivity: Mechanistic Understanding, Successful and Controversial Stories.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Review
- Structural and functional fine mapping of cysteines in mammalian glutaredoxin reveal their differential oxidation susceptibility.Nature communications · 2023Article
- Biological and Catalytic Properties of Selenoproteins.International journal of molecular sciences · 2023Review
- The Key Role of Chalcogenurane Intermediates in the Reduction Mechanism of Sulfoxides and Selenoxides by Thiols Explored In Silico.International journal of molecular sciences · 2023Article
- Diphenyl Diselenide and SARS-CoV-2:Journal of chemical information and modeling · 2023Article
- Analysis and Characterization of Glutathione Peroxidases in an Environmental Microbiome and Isolated Bacterial Microorganisms.Journal of microbiology and biotechnology · 2023Article
- Reactivity and binding mode of disulfiram, its metabolites, and derivatives in SARS-CoV-2 PLJournal of molecular modeling · 2022Article
- Superoxide Radicals in the Execution of Cell Death.Antioxidants (Basel, Switzerland) · 2022Review
- Selenium-Catalyzed Reduction of Hydroperoxides in Chemistry and Biology.Antioxidants (Basel, Switzerland) · 2021Review
- A comparison of Prx- and OxyR-based HThe Journal of biological chemistry · 2021Article
- Effect of Methylmercury Binding on the Peroxide-Reducing Potential of Cysteine and Selenocysteine.Inorganic chemistry · 2021Article
- Looking Back at the Early Stages of Redox Biology.Antioxidants (Basel, Switzerland) · 2020Review
- Antioxidant Potential of Psychotropic Drugs: From Clinical Evidence to In Vitro and In Vivo Assessment and toward a New Challenge for in Silico Molecular Design.Antioxidants (Basel, Switzerland) · 2020Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The (seleno)cysteine residues in some protein families react with hydroperoxides with rate constants far beyond those of fully dissociated low molecular weight thiol or selenol compounds. In case of the glutathione peroxidases, we could demonstrate that high rate constants are achieved by a proton transfer from the chalcogenol to a residue of the active site [Orian et al. Free Radic. Biol. Med. 87 (2015)]. We extended this study to three more protein families (OxyR, GAPDH and Prx). According to DFT calculations, a proton transfer from the active site chalcogenol to a residue within the active site is a prerequisite for both, creating a chalcogenolate that attacks one oxygen of the hydroperoxide substrate and combining the delocalized proton with the remaining OH or OR, respectively, to create an ideal leaving group. The "parking postions" of the delocalized proton differ between the protein families. It is the ring nitrogen of tryptophan in GPx, a histidine in GAPDH and OxyR and a threonine in Prx. The basic principle, however, is common to all four families of proteins. We, thus, conclude that the principle outlined in this investigation offers a convincing explanation for how a cysteine residue can become peroxidatic.
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