Premium
The antiviral protein viperin is a radical SAM enzyme
Author(s) -
Duschene Kaitlin S.,
Broderick Joan B.
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.02.041
Subject(s) - chemistry , iron–sulfur cluster , cleavage (geology) , enzyme , mass spectrometry , electron paramagnetic resonance , cluster (spacecraft) , stereochemistry , biochemistry , biology , chromatography , paleontology , physics , nuclear magnetic resonance , fracture (geology) , computer science , programming language
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.