ArticleProceedings of the National Academy of Sciences of the United States of America2014
Redox active motifs in selenoproteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 64 citations in OpenAlex.
- Unveiling Selenoprotein T as a novel regulator of cardiomyocyte senescence: pivotal role of the CD36 receptor in AC16 human cardiomyocytes.GeroScience · 2026Article
- Can selenenyl sulfides be a substrate of glutathione reductase enzyme? A theoretical insight.RSC advances · 2024Article
- Effects of nanoselenium supplementation on lactation performance, nutrient digestion and mammary gland development in dairy cows.Animal biotechnology · 2024Article
- The redox-active defensive Selenoprotein T as a novel stress sensor protein playing a key role in the pathophysiology of heart failure.Journal of translational medicine · 2024Article
- Selenium status in term neonates, according to birth weight and gestational age, in relation to maternal hypertensive pathology.Frontiers in pediatrics · 2023Article
- Article
- Harnessing selenocysteine to enhance microbial cell factories for hydrogen production.Frontiers in catalysis · 2022Article
- Article
- Differential regulation of cellular stress responses by the endoplasmic reticulum-resident Selenoprotein S (Seps1) in proliferating myoblasts versus myotubes.Physiological reports · 2018Article
- Selenocysteine mimics the effect of dietary restriction on lifespan via SKN‑1 and retards age‑associated pathophysiological changes in Caenorhabditis elegans.Molecular medicine reports · 2018Article
- Sodium Selenite Prevents Paraquat-Induced Neurotoxicity in Zebrafish.Molecular neurobiology · 2018Article
- Antioxidant effects of selenocysteine on replicative senescence in human adipose-derived mesenchymal stem cells.BMB reports · 2017Article
- Selenocysteine modulates resistance to environmental stress and confers anti-aging effects in C. elegans.Clinics (Sao Paulo, Brazil) · 2017Article
- Trifluoroselenomethionine: A New Unnatural Amino Acid.Chembiochem : a European journal of chemical biology · 2016Article
- Review
- The source of circulating selenoprotein S and its association with type 2 diabetes mellitus and atherosclerosis: a preliminary study.Cardiovascular diabetology · 2016Article
- (77)Se chemical shift tensor of L-selenocystine: experimental NMR measurements and quantum chemical investigations of structural effects.The journal of physical chemistry. B · 2015Article
- The intrinsically disordered membrane protein selenoprotein S is a reductase in vitro.Biochemistry · 2013Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Selenoproteins use the rare amino acid selenocysteine (Sec) to act as the first line of defense against oxidants, which are linked to aging, cancer, and neurodegenerative diseases. Many selenoproteins are oxidoreductases in which the reactive Sec is connected to a neighboring Cys and able to form a ring. These Sec-containing redox motifs govern much of the reactivity of selenoproteins. To study their fundamental properties, we have used (77)Se NMR spectroscopy in concert with theoretical calculations to determine the conformational preferences and mobility of representative motifs. This use of (77)Se as a probe enables the direct recording of the properties of Sec as its environment is systematically changed. We find that all motifs have several ring conformations in their oxidized state. These ring structures are most likely stabilized by weak, nonbonding interactions between the selenium and the amide carbon. To examine how the presence of selenium and ring geometric strain governs the motifs' reactivity, we measured the redox potentials of Sec-containing motifs and their corresponding Cys-only variants. The comparisons reveal that for C-terminal motifs the redox potentials increased between 20-25 mV when the selenenylsulfide bond was changed to a disulfide bond. Changes of similar magnitude arose when we varied ring size or the motifs' flanking residues. This suggests that the presence of Sec is not tied to unusually low redox potentials. The unique roles of selenoproteins in human health and their chemical reactivities may therefore not necessarily be explained by lower redox potentials, as has often been claimed.
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