Jeremy Burkett Ph.D.

Research

My research focuses on investigating natural catalytic/enzymatic processes using zeolite frameworks to encapsulate small, low-coordinate metal complexes as simplified mimics of the native systems. Overall protein structures have a synergistic relationship with the metal complexes in the active sites, which in many cases allow reactions to take place that would otherwise be impossible. The physical dimensions of the protein structure can align substrates perfectly for coordination to the active center where bond breakage/formation ultimately takes place. Recent work using zeolite frameworks with encapsulated metal complexes has demonstrated the potential of these systems to be studied as simplified models of complicated natural enzymes. Furthering our understanding of natural enzyme pathways can not only help to expand our fundamental knowledge of the world around us but also allow us to discover new ways to apply that knowledge, by improving existing catalytic systems or even creating new ones altogether.

My research is currently focused on investigating zeolite systems that model nitrogenase enzymes. Nitrogen fixation is a hugely important part of the global ecosystem as well as industrially significant (Haber-Bosch process). Students working on this project are able to be involved at every level of the research, learning and developing the skills of an inorganic chemist. Students will help to identify metal complexes as potential mimics of the natural active sites of nitrogenase enzymes as well as synthesize and purify those targets. Students will also perform calculations to ideally match unique zeolite frameworks to targeted metal complexes. Various encapsulation methods will be investigated and ultimately, students in our lab will perform all catalytic testing of the completed zeolite systems.