Artificial metalloenzymes have emerged as biohybrid catalysts that allow to combine the reactivity of a metal catalyst with the flexibility of protein scaffolds. Here, we report the artificial metalloenzymes based on the β‐barrel protein nitrobindin NB4, in which a cofactor [CoIIX(Me3TACD‐Mal)]+X‐ (X = Cl, Br; Me3TACD = N,N´,N´´‐trimethyl‐1,4,7,10‐tetraazacyclododecane, Mal = CH2CH2CH2NC4H2O2) was covalently anchored via a Michael addition reaction. These biohybrid catalysts showed higher efficiency than the free cobalt complexes for the oxidation of benzylic C(sp3)‐H bonds in aqueous media. Using commercially available oxone (2KHSO5·KHSO4·K2SO4) as oxidant, a total turnover number of up to 220 and 97% ketone selectivity were achieved for tetralin. As catalytically active intermediate, a mononuclear terminal cobalt(IV)‐oxo species [Co(IV)=O]2+ was generated by reacting the cobalt(II) cofactor with oxone in aqueous solution and characterized by ESI‐TOF MS.