Metalloenzymes catalyze the challenging chemical reactions that lie at the core of vital life processes, from carbon and nitrogen fixation to photosynthesis and respiration. Native metalloenzymes use only earth-abundant transition metals and operate under mild conditions, accessing reactivity that remains largely out of reach for synthetic systems. Given the importance of these fundamental processes in the context of energy, environment, sustainability, and human health, gaining molecular-level understanding into how metalloenzymes work is of the utmost importance. We are currently targeting three primary areas within bioinorganic chemistry– protein-based models of hydrogenase enzymes; one-carbon conversion processes catalyzed by nickel metalloproteins; and multielectron oxidative reactivity in heterobimetallic manganese-iron proteins.
To address these challenges, we use a complementary suite of biological, chemical, and physical techniques, as shown below. These methods allow us to study all aspects of metalloenzyme reactivity, from the active site to global dynamical motion and beyond.
