2-ketoglutarate (2-KG)/Fe-dependent dioxygenases can catalyze the highly specific regio- and stereoselective functionalization of C(sp)-H bond of complex compounds under mild reaction conditions. Hyoscyamine 6β-hydroxylase (H6H), a member of these dioxygenases, catalyzes two consecutive oxidation reactions in the synthesis of scopolamine. The first reaction is the hydroxylation of hyoscyamine to 6β-hydroxyhyoscyamine and the second is epoxidation of 6β-hydroxyhyoscyamine. This paper introduces the catalytic mechanism, substrate scope, and application of H6H and evaluates the possibility of this enzyme as a biocatalyst for the functionalization of C(sp)-H bond in complex compounds with different structural characteristics hydroxylation or epoxidation, providing a theoretical basis for modification and application of this enzyme.
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