Abstract
Dihydroxyacetanilide, 4, is oxidized to the 5R,6S-epoxyquinone, 3, by dihydroxyacetanilide epoxidase-I (DHAE I) from Streptomyces LL-C10037, without the assistance of an organic cofactor. 13C NMR analysis revealed that in the presence of 18O2 a full equivalent of 18O is incorporated at the epoxide. However, control reactions revealed the rapid exchange of the C-4 carbonyl with H218O. By coupling the DHAE I reaction with 2-acetamido-5,6-epoxy-1,4-benzoquinone oxidoreductase (AEBQOR I) from the same organism, NADP, and an NADPH regeneration system based on glucose 6-phosphate dehydrogenase, the epoxyquinol LL-C10037α, 1, was produced with ∼20% incorporation of a second 18O atom at the C-4 alcohol. Therefore, DHAE I is a dioxygenase with an epoxidation mechanism essentially the same as has been observed for the dihydrovitamin K epoxidation occurring during the mammalian vitamin K-dependent glutamate carboxylase reaction.
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