title: The antiviral protein viperin is a radical SAM enzyme.
abstract: Viperin, an interferon-inducible antiviral protein, is shown to bind an iron-sulfur cluster, based on iron analysis as well as UV-Vis and electron paramagnetic resonance spectroscopic data. The reduced protein contains a [4Fe-4S](1+) cluster whose g-values are altered upon addition of S-adenosylmethionine (SAM), consistent with SAM coordination to the cluster. Incubation of reduced viperin with SAM results in reductive cleavage of SAM to produce 5'-deoxyadenosine (5'-dAdo), a reaction characteristic of the radical SAM superfamily. The 5'-dAdo cleavage product was identified by a combination of HPLC and mass spectrometry analysis.
authors.affiliation: Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59717, USA.
authors.forename: Kaitlin S
authors.initials: KS
authors.lastname: Duschene
authors.forename: Joan B
authors.initials: JB
authors.lastname: Broderick
mesh_terms: D000998:Antiviral Agents / Q000302:isolation & purification / Q000378:metabolism; D003001:Cloning, Molecular; D006801:Humans; D006867:Hydrolases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism / Q000502:physiology; D006868:Hydrolysis; D066298:In Vitro Techniques; D007501:Iron / Q000378:metabolism; D008954:Models, Biological; D010084:Oxidation-Reduction; D044925:Oxidoreductases Acting on CH-CH Group Donors; D011485:Protein Binding; D011506:Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism / Q000502:physiology*; D012436:S-Adenosylmethionine / Q000737:chemistry / Q000378:metabolism; D013455:Sulfur / Q000378:metabolism; D013997:Time Factors; D000090123:Viperin Protein
chemical_list: D000998:Antiviral Agents; D006867:Hydrolases; D007501:Iron; D044925:Oxidoreductases Acting on CH-CH Group Donors; D011506:Proteins; D012436:S-Adenosylmethionine; D013455:Sulfur; C444427:RSAD2 protein, human; D000090123:Viperin Protein; C019614:adenosylmethionine hydrolase