Superactivity of Bimetallic CuFeO₂ Submicron Particles towards Selective Proteolysis, Depending on their Surface Hydroxyls

Nano bimetallic oxides as nanoproteases have the great advantages in the heterogeneous hydrolysis of proteins. Here, we report that bimetallic delafossite CuFeO 2 submicron particles (CuFeO 2 SMPs) display a high protease activity towards selective cleavage of peptide bond involving hydrophobic residue at 25 °C. CuFeO 2 SMPs have excellent r egeneration performance with high structural stability. The strong Lewis acidity of Fe 3+ and the strong nucleophilicity of Cu + bound hydroxyl groups are both necessary for the high protease activity of CuFeO 2 SMPs. Low‐valent metal ion has a great advantage in that low‐valent Cu + bound hydroxyl has strong nucleophilicity, resulting in promotion of protein hydrolysis via high‐efficient bimetallic catalysis . This study provides evidence that the protease activity of CuFeO 2 SMPs depends on metal ion‐bound hydroxyls on their surface. Our findings highlight that the valence of metal ions in artificial protease and their surface hydroxyls are two important factors that determine their catalytic efficiency.