Selenium utilization in thioredoxin and catalytic advantage provided by selenocysteine

The thioredoxin antioxidant system

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Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide.

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How Selenium Has Altered Our Understanding of the Genetic Code

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The structure of the mouse glutathione peroxidase gene: the selenocysteine in the active site is encoded by the ‘termination’ codon, TGA.

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Thiol redox control via thioredoxin and glutaredoxin systems

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M ECHANISM AND R EGULATION OF S ELENOPROTEIN S YNTHESIS

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Methionine Sulfoxide Reduction in Mammals: Characterization of Methionine- R -Sulfoxide Reductases

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Mammalian thioredoxin reductase: Oxidation of the C-terminal cysteine/selenocysteine active site forms a thioselenide, and replacement of selenium with sulfur markedly reduces catalytic activity

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Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase

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High-level expression in Escherichia coli of selenocysteine-containing rat thioredoxin reductase utilizing gene fusions with engineered bacterial-type SECIS elements and co-expression with the selA , selB and selC genes 1 1Edited by M. Gottesman

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Dynamic evolution of selenocysteine utilization in bacteria: a balance between selenoprotein loss and evolution of selenocysteine from redox active cysteine residues

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An algorithm for identification of bacterial selenocysteine insertion sequence elements and selenoprotein genes

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The nature of the minimal 'selenocysteine insertion sequence' (SECIS) in Escherichia coli

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Glycine reductase mechanism

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Catalytic Advantages Provided by Selenocysteine in Methionine-S-Sulfoxide Reductases

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The efficiency of Escherichia coli selenocysteine insertion is influenced by the immediate downstream nucleotide

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Highly Conserved Surface Proteins of Oral Spirochetes as Adhesins and Potent Inducers of Proinflammatory and Osteoclastogenic Factors

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Glutaredoxin serves as a reductant for methionine sulfoxide reductases with or without resolving cysteine

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Selenocysteine insertion directed by the 3'-UTR SECIS element in Escherichia coli

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Tandem use of selenocysteine: adaptation of a selenoprotein glutaredoxin for reduction of selenoprotein methionine sulfoxide reductase

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Selenium-dependent growth of Treponema denticola : evidence for a clostridial-type glycine reductase

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Trace elements at the intersection of marine biological and geochemical evolution

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A Facile Method for Producing Selenocysteine‐Containing Proteins

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The physiology and evolution of microbial selenium metabolism

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Selenium Metabolism and Selenoproteins in Prokaryotes: A Bioinformatics Perspective

Zhang, Y., Jin, J., Huang, B., Ying, H., He, J., & Jiang, L. (2022) · Biomolecules · doi:10.3390/biom12070917 · Cited by 31 · see citing works

Probing the active site tryptophan ofStaphylococcus aureusthioredoxin with an analog

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Toxicological effects of CdSe nanocrystals on the marine diatom Phaeodactylum tricornutum: The first mass spectrometry-based proteomic approach

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Ability of the marine bacterium Pseudomonas fluorescens BA3SM1 to counteract the toxicity of CdSe nanoparticles

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Bacteria Versus Selenium: A View from the Inside Out

Staicu, L. C., Oremland, R. S., Tobe, R., & Mihara, H. (2017) · Plant ecophysiology · doi:10.1007/978-3-319-56249-0_6 · Cited by 17 · see citing works

SPARC paucity alleviates superoxide-mediated oxidative stress, apoptosis, and autophagy in diabetogenic hepatocytes

Aseer, K. R., Silvester, A. J., Kumar, A., Choi, M., & Yun, J. W. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.05.011 · Cited by 17 · see citing works

Exploring the selenium-over-sulfur substrate specificity and kinetics of a bacterial selenocysteine lyase

Johnstone, M. A., Nelson, S. J., O’Leary, C., & Self, W. T. (2021) · Biochimie · doi:10.1016/j.biochi.2021.01.002 · Cited by 13 · see citing works

Transcriptomic Responses of Four Pelagophytes to Nutrient (N, P) and Light Stress

Kang, Y., Harke, M. J., Berry, D. L., Collier, J. L., Wilhelm, S. W., Dyhrman, S. T., & Gobler, C. J. (2021) · Frontiers in Marine Science · doi:10.3389/fmars.2021.636699 · Cited by 11 · see citing works

Eine einfache Methode zur Produktion von Selenoproteinen

Mukai, T., Sevostyanova, A., Suzuki, T., Fu, X., & Söll, D. G. (2018) · Angewandte Chemie · doi:10.1002/ange.201713215 · Cited by 5 · see citing works

Prokaryotic Selenoproteins and Selenoproteomes

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Ancient Loss of Catalytic Selenocysteine Spurred Convergent Adaptation in a Mammalian Oxidoreductase

Rees, J., Sarangi, G. K., Cheng, Q., Floor, M., Andrés, A. M., Oliva, B., Villà­-Freixa, J., Arnér, E. S. J., & Castellano, S. (2024) · Genome Biology and Evolution · doi:10.1093/gbe/evae041 · Cited by 2 · see citing works

Recent advances in exploring the composition and evolution of the prokaryotic selenoproteome

Zhang, Y., Wang, S., Li, H., & Chen, X. (2026) · Applied and Environmental Microbiology · doi:10.1128/aem.00556-26 · Cited by 1 · see citing works

Non-standard amino acid incorporation into thiol dioxygenases

Bennett, Z., & Brunold, T. C. (2024) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2024.05.022 · Cited by 1 · see citing works

The Physiology and Evolution of Selenite Respiration in Bacteria

Wells, M. (2020) · Cited by 1 · see citing works

Selenium vs. Sulfur: Investigating the Substrate Specificity of a Selenocysteine Lyase

Johnstone, M. (2019) · Journal of International Crisis and Risk Communication Research

Selenocysteine and Selenoproteins

Cohen, G. N. (2016) · Springer eBooks · doi:10.1007/978-94-017-7579-3_30

Selenium Bioavailability in Food and the Impact in Mammals Gut Microbiota

Leblic, B. C., Arias‐Borrego, A., Vélez-Pérez, R. D. F., & García‐Barrera, T. (2025) · Environmental science and engineering · doi:10.1007/978-3-031-93957-0_28

Physiology combined with transcriptomics and 16S rRNA profiling reveals the regulation of winter wheat's adaptability to saline-alkali land by foliar spraying of selenium nanoparticles

Fan, G., Chao, K., & Shi, Y. (2026) · Plant and Soil · doi:10.1007/s11104-026-08340-x

Selenium Neurotoxicity and Nutritional Signaling: Integrated Oxidative Stress Pathways in C. elegans

Mukem, S., Somkasetrin, A., Thongsroy, J., Tan, J., Srichai, B., & Chuaijit, S. (2026) · Stresses · doi:10.3390/stresses6010015

Essential Role of Selenium in the Catalytic Activities of Mammalian Thioredoxin Reductase Revealed by Characterization of Recombinant Enzymes with Selenocysteine Mutations

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Active sites of thioredoxin reductases: Why selenoproteins?

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Lcms-Based Analysis Explains The Basis Of Oxidative Resistance In Selenium-Containing Thioredoxin Reductase

Haupt, D. J. (2021) · ScholarWorks -A service of University of Vermont Libraries (University of Vermont)

Evidence for a functional relevance of the selenocysteine residue in mammalian thioredoxin reductase

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Why Is Mammalian Thioredoxin Reductase 1 So Dependent upon the Use of Selenium?

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