Welcome to the Borovik Group


As an inorganic chemistry group, we are interested in the features of metalloprotein active sites that facilitate their highly selective and efficient functions. Unraveling the intricate workings of these systems is a challenging endeavor, given their complexity. In particular, we are inspired by key architectural features found in the secondary coordination spheres of metalloprotein active sites such as hydrogen bonding (H-bonds) and their influence on reactivity. To study these features in detail, our group has developed innovative design approaches to manipulate the local environments surrounding metal centers. One approach has been the preparation and characterization of synthetic constructs designed to emulate aspects of native metalloproteins, with a particular focus on controlling factors in the secondary coordination sphere. These synthetic systems enable the dissection of individual structural components and their impact on function, allowing us to establish crucial structure-function correlations vital for mechanistic evaluations. Over the past several years, we have expanded our synthetic toolbox through a chemogenetic approach as another method to control the microenvironment surrounding a metal ion. Here, chemical synthesis of biotinylated ligands allows us to anchor the resultant metal complexes into a protein host. Through genetic manipulation of this host, we can systematically modulate the covalent and noncovalent interactions incurred between amino acid side chains and the metal ion(s)

Active Research Areas

Small Molecule Activation

Hydrogen bonding interactions influence the secondary coordination spheres of metal ions in proteins.  To emulate these architectures, we design and develop synthetic complexes with tunable hydrogen bonding motifs.

Artificial Metalloproteins

Our semi-synthetic approach incorporates biotinylated metal complexes into a protein host, Streptavadin, which are further manipulated through mutagenesis of the surrounding amino acids. Combining parallel structural and spectroscopic methods, we characterize ArMs in both their resting and activated states to mimic aspects of naturally occurring metalloproteins that are challenging to trap by traditional methods.