Research Description

The Slater Lab is interested in how metalloenzymes accomplish chemistry that remains difficult for synthetic catalysts. Iron- and copper-dependent enzymes activate oxygen, break strong C-H bonds, and assemble unusual functional groups under mild conditions. Our goal is to understand the catalytic mechanisms that make this possible: which intermediates form along a reaction coordinate, what each one contributes to the chemistry, and how the enzyme controls the sequence. Because these species often persist for only milliseconds, answering those questions requires catching them in the act. Once an intermediate is characterized, it becomes something we can act on. Perturbing it, stabilizing it, or redirecting it is how we test our understanding of a mechanism and how we begin to steer a reaction toward chemistry the enzyme does not natively perform.

Understanding an enzyme well enough to redirect it also means understanding where it is weakest. Many bacterial pathogens depend on their own metalloenzymes to survive within a host, and the intermediates that make those enzymes effective can also make them vulnerable. We are working to identify small molecules that exploit that vulnerability, using mechanistic insight to guide the search for new antibiotics.

Our approach pairs transient kinetics with the core spectroscopies of the bioinorganic toolbox: UV-visible and infrared absorption, resonance Raman, electron paramagnetic resonance (EPR), and Mössbauer. Each reports on a different aspect of the system, and together they allow us to follow a reaction as it proceeds while resolving the structure and electronic state of the species carrying it out.

Frequently the measurement we need is not one a commercial instrument is built to make. In the Slater Lab, we design and build the hardware that closes that gap: gas manifolds, sample manipulators, cryogenic handling systems, 3D-printed adapters and fixtures, and new approaches to stopped-flow and rapid freeze-quench sample preparation.