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The Elusive 5′-Deoxyadenosyl Radical: Captured and Characterized by EPR and ENDOR Spectroscopies

preprint
submitted on 07.06.2019, 20:31 and posted on 10.06.2019, 19:03 by Hao Yang, Elizabeth C. McDaniel, Stella Impano, Amanda S. Byer, Richard Jodts, Kenichi Yokoyama, William E. Broderick, Joan Broderick, Brian M. Hoffman
The 5'-deoxyadenosyl radical (5'-dAdo•) abstracts a substrate H-atom as the first step in radical-based transformations catalyzed by adenosylcobalamin-dependent and radical S-adenosyl-l-methionine (RS) enzymes. Notwithstanding its central biological role, 5'-dAdo• has eluded characterization despite efforts spanning more than a half-century. Here we report generation of 5'-dAdo• in a RS enzyme active site at 12 K, using a novel approach involving cryogenic photoinduced electron transfer from the [4Fe-4S]+cluster to the coordinated S-adenosylmethionine (SAM) to induce homolytic S-C' bond cleavage.

Funding

NIH GM 111097

NIH GM 54608

History

Email Address of Submitting Author

jbroderick@montana.edu

Institution

Montana State University

Country

USA

ORCID For Submitting Author

0000-0001-7057-9124

Declaration of Conflict of Interest

No conflict of interest.

Version Notes

June 7, 2019

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in Journal of the American Chemical Society

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