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

preprint
submitted on 07.06.2019 and posted on 10.06.2019 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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