ArticleJournal of the American Chemical Society2006
Synthetic seleno-glutaredoxin 3 analogues are highly reducing oxidoreductases with enhanced catalytic efficiency.
Article in Journal of the American Chemical Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 143 citations in OpenAlex.
- Semi-synthesis of the C-terminal region ofRSC chemical biology · 2026Article
- Lipid Quality Control and Ferroptosis: From Concept to Mechanism.Annual review of biochemistry · 2024Review
- Seleno-relaxin analogues: effect of internal and external diselenide bonds on the foldability and a fibrosis-related factor of endometriotic stromal cells.RSC chemical biology · 2024Article
- Selenium chemistry for spatio-selective peptide and protein functionalization.Nature reviews. Chemistry · 2024Review
- Design, synthesis, conformational analysis, and biological activity of CαJournal of enzyme inhibition and medicinal chemistry · 2023Article
- Diselenide-bond replacement of the external disulfide bond of insulin increases its oligomerization leading to sustained activity.Communications chemistry · 2023Article
- Chemical synthesis of human selenoprotein F and elucidation of its thiol-disulfide oxidoreductase activity.Chemical science · 2022Article
- One-Pot Chemical Protein Synthesis Utilizing Fmoc-Masked Selenazolidine to Address the Redox Functionality of Human Selenoprotein F.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Selenium-Catalyzed Reduction of Hydroperoxides in Chemistry and Biology.Antioxidants (Basel, Switzerland) · 2021Review
- General lack of structural characterization of chemically synthesized long peptides.Protein science : a publication of the Protein Society · 2019Review
- Gain of function conferred by selenocysteine: catalytic enhancement of one-electron transfer reactions by thioredoxin reductase.Protein science : a publication of the Protein Society · 2019Article
- Selenocysteine-Mediated Expressed Protein Ligation of SELENOM.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Utilizing Selenocysteine for Expressed Protein Ligation and Bioconjugations.Journal of the American Chemical Society · 2017Article
- Accessing human selenoproteins through chemical protein synthesis.Chemical science · 2017Article
- Future of the Genetic Code.Life (Basel, Switzerland) · 2017Review
- Synthesis and activity of a diselenide bond mimetic of the antimicrobial protein caenopore-5.Chemical science · 2016Article
- Insights into the deselenization of selenocysteine into alanine and serine.Chemical science · 2015Article
- Fmoc-Sec(Xan)-OH: synthesis and utility of Fmoc selenocysteine SPPS derivatives with acid-labile sidechain protection.Journal of peptide science : an official publication of the European Peptide Society · 2015Article
- Selenoprotein K form an intermolecular diselenide bond with unusually high redox potential.FEBS letters · 2014Article
- Redox active motifs in selenoproteins.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
Selenoenzymes have a central role in maintaining cellular redox potential. These enzymes have selenenylsulfide bonds in their active sites that catalyze the reduction of peroxides, sulfoxides, and disulfides. The selenol/disufide exchange reaction is common to all of these enzymes, and the active site redox potential reflects the ratio between the forward and reverse rates of this reaction. The preparation of enzymes containing selenocysteine (Sec) is experimentally challenging. As a result, little is known about the kinetic role of selenols in enzyme active sites, and the redox potential of a selenenylsulfide or diselenide bond in a protein has not been experimentally determined. To fully evaluate the effects of Sec on oxidoreductase redox potential and kinetics, glutaredoxin 3 (Grx3) and all three Sec variants of its conserved (11)CXX(14)C active site were chemically synthesized. Grx3, Grx3(C11U), and Grx3(C14U) exhibited redox potentials of -194, -260, and -275 mV, respectively. The position of redox equilibrium between Grx3(C11U-C14U) (-309 mV) and thioredoxin (Trx) (-270 mV) suggests a possible role for diselenide bonds in biological systems. Kinetic analysis is consistent with the hypothesis that the lower redox potentials of the Sec variants result primarily from the greater nucleophilicity of the active site selenium rather than its role as either a leaving group or a "central atom" in the exchange reaction. The 10(2)-10(4)-fold increase in the rate of Trx reduction by the seleno-Grx3 analogues demonstrates that oxidoreductases containing either selenenyl-sulfide or diselenide bonds can have physiologically compatible redox potentials and enhanced reduction kinetics in comparison with their sulfide counterparts.
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