A series of high-spin iron(III) complexes, {N-R-2-[(pyridin-2-ylmethyl)amino]acetamide}FeCl3 [R = mesityl (1b), 2,6-Et2C6H3 (2b), and 2,6-i-Pr2C6H3 (3b)], that functionally emulate the intradiol catechol dioxygenase enzyme are reported. In particular, these enzyme mimics, 1b, 2b, and 3b, which utilized molecular oxygen in carrying out the intradiol catechol cleavage of 3,5-di-tert-butylcatechol with high regioselectivity. (ca. 81-85%) at room temperature under ambient conditions, were designed by employing a new class of a facially bound [N2O] ligand, namely, N-R-2-[(pyridin-2-ylmethyl)amino]acetamide [R = mesityl (1a), 2,6-Et2C6H3 (2a), and 2,6-i-Pr2C6H3 (3a)]. The density functional theory studies revealed that the intradiol catechol cleavage reaction proceeded by an iron(III) peroxo intermediate that underwent 1,2-Criegee rearrangement to yield the intradiol catechol cleaved products analogous to the native enzyme.