Oxygenase enzymes constitute a class of oxidoreductases that catalyze the direct incorporation of one or both atoms of molecular oxygen (O₂) into organic substrates, thereby oxidizing the substrate through a bona fide oxygen-transfer mech^[1]anism rather than through electron or hydrogen abstraction ^[2]. In the Enzyme Commission nomenclature, oxygenases are assigned to EC 1.13 (acting on single donors with incorporation of molecular oxygen) and EC 1.14 (acting on paired donors with incorporation or reduction of molecular oxygen) ^[3]. The class is partitioned into two functional categories according to oxygen stoichiometry: monooxygenases incorporate one atom of O₂ into the substrate while reducing the second oxygen atom to water, whereas dioxygenases incorporate both atoms of molecular oxygen into the substrate . Catalysis by oxygenases generally requires reductive activation of O₂ at a redox-active metal center or organic cofactor, with heme iron, flavin, mononuclear non-heme iron, Rieske iron–sulfur clusters, and Fe(II)/2-oxoglutarate centers representing the principal cofactor systems that support substrate oxygenation ^[4][5]. The essential components of an oxygenase-catalyzed reaction are therefore the catalytic cofactor or metal center, the organic substrate that accepts the oxygen atom(s), and, for many members, an electron-delivery system that sustains the reduced cofactor state required for O₂ activation ^[3][4].