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Heidinger, Lorenz, Kneuttinger, Andrea C., Kashiwazaki, Gengo, Weber, Stefan, Carell, Thomas and Schleicher, Erik (2016): Direct observation of a deoxyadenosyl radical in an active enzyme environment. In: Febs Letters, Vol. 590, No. 24: pp. 4489-4494

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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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