Enzyme-mimicking of copper-sites in metal-organic frameworks for oxidative degradation of phenolic compounds

Two on the main factors that control the activity and selectivity of the metal sites within metalloenzymes are: (i) their coordination environments, and the (ii) number and connectivity of the metal ions in the active site (i.e. nuclearity). This is the archetypal example of copper metalloproteins, as specifically of laccases and copper oxidases. Here we show that metal-organic frameworks can be used to install amino acid-copper sites with a partial control over their coordination environment and nuclearity of the final site. The activity of our bioinspired MOF-808@(amino)acid-copper catalysts have been assessed over the wet oxidation of phenolic pollutants. Our results demonstrate a clear modulation of the catalytic efficiency and selectivity of the copper-sites controlled by the coordination-sphere and their clustering degree. We anticipate that the approach presented in this work can be the starting point for more sophisticated reconstruction of enzyme active sites with regioselective activities. Two of the main factors controlling the activity and selectivity of metal sites within MOF-like copper metalloenzymes are: (i) their coordination environments, and (ii) the number and connectivity of metal ions at the active site (i.e., nuclearity).