Mononuclear non-heme iron enzymes catalyze hydroxylation reaction in the catabolism of biological and environmental compounds. Additionally, they also catalyze a wide range of noncanonical and synthetically challenging reactions to install functional groups and introduce structural complexity in natural products. Despite this chemical diversity, all non-heme iron and 2-oxoglutarate dependent enzymes studied to date employ a high-valent iron-oxo species to enable hydrogen atom abstraction, a.k.a. C-H activation, from an otherwise inert C–H bond. Much less understood is how the fate of the resulting substrate radical is controlled leading to oxygen rebound process and thus leading to hydroxylation outcome versus alternative reaction outcomes including C-C and C-N bond forming reactions. Herein, we demonstrate that the position and orientation of the iron-oxo species relative to the substrate and an assisting group of the substrate not only perturb the lifetime of the iron-oxo species, but also facilitate the formation of cyclopropane, cyclohexane and isonitrile moieties. These results provide mechanistic insights into the development of mononuclear non-heme iron enzymes to enable noncanonical reactivities.