Non-heme iron enzymes catalyze a broad array of reactions for a large number of biomedically, and agriculturally important oxidation reactions. Protein ligand sets as minimal as a pair of histidines and an aspartate (or glutamate) enable the iron center to coordinate in the active site, leading to ferryl intermediate formation via reacting with molecular oxygen and 2-oxoglutarate. Many of these reactions install key functional groups in natural product biosynthesis. In the past few years, we have elucidated plausible pathways in various functional group installation. In addition to hydroxylation, as it results from coupling between the carbon radical and the Fe(III)-OH, the substrate radical can utilize different strategies to redirect the reaction outcome. From a few systems we studied, it can be achieved by not only substrate pocket binding but also by providing a compelling pathway to redirect reaction outcome. To understand these reactions, it is important to utilize complementary approach to visualize intermediates through the reaction sequences.