Abstract: 

Nature performs challenging chemical transformations with the help of metalloenzymes. The efficiency and selectivity of such reactions has been attributed to the control of the covalent as well as non-covalent interactions around the metal center. In synthetic systems, it has been difficult to emulate the long-range non-covalent interactions that are found in native enzymes. To incorporate such non-covalent interactions into the modeling of the active sites of metalloenzymes, biotin-streptavidin (Sav) technology has been utilized to immobilize metal complexes within the protein scaffold. This dissertation describes my efforts in engineering artificial metalloproteins (ArMs) using biotin-Sav technology to install non-heme iron active sites that are capable of binding to small molecules.