ArticleMethods in enzymology2022
Selenocysteine substitutions in thiyl radical enzymes.
Article in Methods in enzymology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 8 citations in OpenAlex.
- Nitric Oxide Inhibition of Glycyl Radical Enzymes and Their Activases.Journal of the American Chemical Society · 2025Article
- Non-standard amino acid incorporation into thiol dioxygenases.Methods in enzymology · 2024Article
- The Mechanism of Inhibition of Pyruvate Formate Lyase by Methacrylate.Journal of the American Chemical Society · 2023Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Cysteine thiyl radicals are implicated as cofactors in a variety of enzymatic transformations, as well as transient byproducts of oxidative stress, yet their reactivity has undermined their detailed study. Selenocysteine exhibits a lower corresponding selenyl radical reduction potential, thus taming this radical reactivity without significant steric perturbation, potentially affording a glimpse into otherwise fleeting events in thiyl radical catalysis. In this chapter, we describe a suite of fusion protein constructs for general and efficient production of site-specifically incorporated selenoproteins by a recently developed nonsense suppression technology. As a proof of concept, we produced NikJ, a member of the radical S-adenosyl methionine enzyme family involved in the biosynthesis of peptidyl nucleoside antibiotics. We place emphasis throughout the plasmid assembly, protein expression, and selenium quantitation on accommodating the structural and functional diversity of thiyl radical enzymes. The protocol produces NikJ with near quantitative selenocysteine insertion, 50% nonsense read-through, and facile protein purification.
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