Regioselective aromatic hydroxylation is desirable for the production of valuable compounds. External flavin‐containing monooxygenases activate and selectively incorporate an oxygen atom in phenolic compounds through flavin reduction by the nicotinamide adenine dinucleotide coenzyme and subsequent reaction with molecular oxygen. This study provides the proof of principle of flavoenzyme‐catalyzed selective aromatic hydroxylation with coenzyme biomimetics. The carbamoylmethyl‐substituted biomimetic in particular affords full conversion in less than two hours for the selective hydroxylation of 5 mM 3‐ and 4‐hydroxybenzoates, displaying similar rates as with NADH, achieving a 10 mM/h enzymatic conversion of the medicinal product gentisate. This biomimetic appears to generate less uncoupling of hydroxylation that typically leads to undesired hydrogen peroxide. Therefore, we show these flavoenzymes have the potential to be applied in combination with biomimetics.