ArticleMolecular microbiology2011
Tandem use of selenocysteine: adaptation of a selenoprotein glutaredoxin for reduction of selenoprotein methionine sulfoxide reductase.
Article in Molecular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 24 citations in OpenAlex.
- Recent advances in exploring the composition and evolution of the prokaryotic selenoproteome.Applied and environmental microbiology · 2026Review
- Selenium Metabolism and Selenoproteins in Prokaryotes: A Bioinformatics Perspective.Biomolecules · 2022Review
- Monothiol and dithiol glutaredoxin-1 fromIUCrJ · 2020Article
- The Oxidized Protein Repair Enzymes Methionine Sulfoxide Reductases and Their Roles in Protecting against Oxidative Stress, in Ageing and in Regulating Protein Function.Antioxidants (Basel, Switzerland) · 2018Review
- Selenium utilization in thioredoxin and catalytic advantage provided by selenocysteine.Biochemical and biophysical research communications · 2015Article
- Evidence for the dimerization-mediated catalysis of methionine sulfoxide reductase A from Clostridium oremlandii.PloS one · 2015Article
- Essential role of the C-terminal helical domain in active site formation of selenoprotein MsrA from Clostridium oremlandii.PloS one · 2015Article
- The methionine sulfoxide reduction system: selenium utilization and methionine sulfoxide reductase enzymes and their functions.Antioxidants & redox signaling · 2013Review
- Evaluation of a dithiocarbamate derivative as an inhibitor of human glutaredoxin-1.Journal of enzyme inhibition and medicinal chemistry · 2013Article
- A novel protein kinase-like domain in a selenoprotein, widespread in the tree of life.PloS one · 2012Article
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Authors and funding
7 authors at 6 institutions in 2 countries.
Funding
Abstract
Several engineered selenocysteine (Sec)-containing glutaredoxins (Grxs) and their enzymatic properties have been reported, but natural selenoprotein Grxs have not been previously characterized. We expressed a bacterial selenoprotein Grx from Clostridium sp. (also known as Alkaliphilus oremlandii) OhILAs in Escherichia coli and characterized this selenoenzyme and its natural Cys homologues in Clostridium and E. coli. The selenoprotein Grx had a 200-fold higher activity than its Sec-to-Cys mutant form, suggesting that Sec is essential for catalysis by this thiol-disulfide oxidoreductase. Kinetic analysis also showed that the selenoprotein Grx had a 10-fold lower K(m) than Cys homologues. Interestingly, this selenoenzyme efficiently reduced a Clostridium selenoprotein methionine sulfoxide reductase A (MsrA), suggesting that it is the natural reductant for the protein that is not reducible by thioredoxin, a common reductant for Cys-containing MsrAs. We also found that the selenoprotein Grx could not efficiently reduce a Cys version of Clostridium MsrA, whereas natural Clostridium and E. coli Cys-containing Grxs, which efficiently reduce Cys-containing MsrAs, poorly acted on the selenoprotein MsrA. This specificity for MsrA reduction could explain why Sec is utilized in Clostridium Grx and more generally provides a novel example of the use of Sec in biological systems.
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