Elaborations of unactivated carbon centers are among the most demanding reactions that enzymes catalyze. These reactions generally involve radical intermediates, often produced by strategic abstraction of substrate hydrogen atoms (H�s). A distinct strategy, predominant in the anaerobic world and also important in aerobes, employs a 5'-deoxyadenosyl 5'-radical (5'-dA�), derived from a reductive cleavage of S-adenosylmethionine, as the H� abstractor. In all enzymatic reactions in which H� abstraction from an unactivated carbon center has been demonstrated unequivocally, the carbon center has been sp3-hybridized. However, reactions involving the functionalization of sp2-hybridized carbons centers are increasingly observed, especially within the radical SAM superfamily of enzymes. This presentation will highlight unique strategies employed by radical SAM enzymes to functionalize sp2-hybridized carbon centers, with particular focus on RlmN and Cfr, which catalyze the methylation of carbons 2 and 8, respectively, of adenosine 2503 in 23S rRNA. Although C2 methylation is found widely in bacteria and is believed to enhance the fidelity of translation, C8 methylation renders bacteria resistant to a number of antibiotics that target the bacterial ribosome.

Award Address  (Arthur C. Cope Scholar Award (CSM) sponsored by the Arthur C. Cope Fund). Enzymatic functionalization of <i>sp<sup>2</sup></i>-hybridized carbon centers

244th National Meeting (2012)

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Award Address (Arthur C. Cope Scholar Award (CSM) sponsored by the Arthur C. Cope Fund). Enzymatic functionalization of sp2-hybridized carbon centers

Award Address (Arthur C. Cope Scholar Award (CSM) sponsored by the Arthur C. Cope Fund). Enzymatic functionalization of sp²-hybridized carbon centers