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  • Title: Direct observation of a deoxyadenosyl radical in an active enzyme environment.
    Author: Heidinger L, Kneuttinger AC, Kashiwazaki G, Weber S, Carell T, Schleicher E.
    Journal: FEBS Lett; 2016 Dec; 590(24):4489-4494. PubMed ID: 27878994.
    Abstract:
    5'-deoxyadenosyl radicals have been proposed as the first common intermediate in the molecular reaction mechanism of the family of radical S-adenosyl-l-methionine (SAM) enzymes. However, this radical species has not yet been directly observed in a catalytically active enzyme environment. In a reduced and SAM-containing C140A mutant of the spore photoproduct lyase from Geobacillus thermodenitrificans, a mutant with altered catalytic activity, we were able to identify an organic radical with pronounced hyperfine structure using electron paramagnetic resonance spectroscopy. Guided by quantum-chemical computations at the density functional theory level of theory, this radical could be tentatively assigned to a deoxyadenosyl radical, which provides first experimental evidence for this intermediate in the reaction mechanism of radical SAM enzymes.
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