Ontology highlight
ABSTRACT:
SUBMITTER: Yang H
PROVIDER: S-EPMC6784836 | biostudies-literature | 2019 Jul
REPOSITORIES: biostudies-literature
Yang Hao H McDaniel Elizabeth C EC Impano Stella S Byer Amanda S AS Jodts Richard J RJ Yokoyama Kenichi K Broderick William E WE Broderick Joan B JB Hoffman Brian M BM
Journal of the American Chemical Society 20190722 30
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 <i>S</i>-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 f ...[more]