Research in the Kodanko laboratory focuses on the development of metal complexes for protein targeting.  One major area of interest in our laboratory is designing catalytic enzyme inhibitors. Today, most enzyme inhibitors act in a stoichiometric fashion, where one inhibitor molecule interacts with its target protein one molecule at a time. Our goal is to develop new inhibitors that can modify proteins catalytically and selectively. This catalytic strategy would make reagents that target proteins effective at lower concentrations, which could minimize off-target activity. Successful implementation of the catalytic strategy in chemical biology would aid the study of protein function, by furnishing highly potent molecules that block the function of a particular protein. In terms of drug development, the catalytic strategy could one day lower dosage amounts and eliminate side effects when compared with conventional drugs. We consider the metalloantibiotic bleomycin (BLM) a model for our work in this area. Used for decades in cancer chemotherapy, BLM can catalytically degrade DNA in the presence of Fe(II) and O₂. In particular, we are interested in using high-valent iron(IV)-oxo species, also known as ferryls, for protein targeting. Ferryls have the ability to oxidize organic molecules selectively. Having established that ferryls can oxidize the backbone and side chains of amino acids, our group is now applying synthetic chemistry towards the creation of inhibitors that generate ferryl species for selective enzyme inactivation.