Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 137, Issue 21, Pages 6912-6919Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.5b03370
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- Pennsylvania State University
- National Institutes of Health [GM-69657]
- National Science Foundation [MCB-642058, CHE-724084]
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The iron(II)- and 2-(oxo)glutarate-dependent (Fe/2OG) oxygenases catalyze an array of challenging transformations, but how individual members of the enzyme family direct different outcomes is poorly understood. The Fe/2OG halogenase, SyrB2, chlorinates C4 of its native substrate, l-threonine appended to the carrier protein, SyrB1, but hydroxylates C5 of l-norvaline and, to a lesser extent, C4 of l-aminobutyric acid when SyrB1 presents these non-native amino acids. To test the hypothesis that positioning of the targeted carbon dictates the outcome, we defined the positions of these three substrates by measuring hyperfine couplings between substrate deuterium atoms and the stable, EPR-active ironnitrosyl adduct, a surrogate for reaction intermediates. The Fe-H-2 distances and N-Fe-H-2 angles, which vary from 4.2 angstrom and 85 degrees for threonine to 3.4 angstrom and 65 degrees for norvaline, rationalize the trends in reactivity. This experimental correlation of position to outcome should aid in judging from structural data on other Fe/2OG enzymes whether they suppress hydroxylation or form hydroxylated intermediates on the pathways to other outcomes.
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