Enzymes are natural catalysts that can be tuned by directed evolution to generate efficient biocatalyst. Controlling the stereochemical outcome of radical-mediated reactions has been a challenge in synthetic chemistry and asymmetric catalysis. Efficient synthesis of unique antibacterial compounds is a growing demand due to the increase of antibiotic resistant bacteria. By repurposing a cytochrome P450 metalloenzyme, featuring a first-row transition- metal cofactor with redox properties, the chemoenzymatic synthesis of difluorinated bioisostere of oxazolidinone antibiotics can be controlled to aid in the antibiotic resistance crisis. Exchanging the oxygen atom from an oxazolidinone, such as linezolid (Zyvox^TM), to a CF₂ unit enhances desired biological and physical properties without making significant changes to the chemical structure. A CF₂ unit is medicinally important with complementary bioactivity and bioavailability to an oxygen atom. We developed synthetic routes for fluorinated antibiotics using engineered enzymes to catalyze a key, stereocenter forming, radical cyclization step intermediate. Proceeding with synthetic cross-coupling reactions to yield the desired difluorinated bioisostere antibiotic product.