title: Natural and synthetic selenoproteins.
abstract: Once considered highly toxic, the element selenium is now recognized as a micronutrient essential for human health. It is inserted co-translationally into many proteins as the non-canonical amino acid selenocysteine, providing the resulting selenoprotein molecules with a range of valuable redox properties; selenocysteine is also increasingly exploited as a structural and mechanistic probe in synthetic peptides and proteins. Here we review topical investigations into the preparation and characterization of natural and artificial selenoproteins. Such molecules are uniquely suited as tools for protein chemistry and as a test bed for studying novel catalytic activities.
authors.affiliation: Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem 91904, Israel. Electronic address: metanis@mail.huji.ac.il.
authors.forename: Norman
authors.initials: N
authors.lastname: Metanis
authors.affiliation: Laboratory of Organic Chemistry, ETH Zürich, 8093 Zürich, Switzerland. Electronic address: hilvert@org.chem.ethz.ch.
authors.forename: Donald
authors.initials: D
authors.lastname: Hilvert
mesh_terms: D000818:Animals; D006801:Humans; D010084:Oxidation-Reduction; D014176:Protein Biosynthesis; D017510:Protein Folding; D011994:Recombinant Proteins / Q000138:chemical synthesis / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017279:Selenocysteine / Q000138:chemical synthesis / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D051140:Selenoproteins / Q000138:chemical synthesis / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D011994:Recombinant Proteins; D051140:Selenoproteins; D017279:Selenocysteine