Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10872060 | FEBS Letters | 2010 | 5 Pages |
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 5â²-deoxyadenosine (5â²-dAdo), a reaction characteristic of the radical SAM superfamily. The 5â²-dAdo cleavage product was identified by a combination of HPLC and mass spectrometry analysis.
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Authors
Kaitlin S. Duschene, Joan B. Broderick,