M. Singleton's research description
How can we compete with enzymes? Enzymes have evolved methods to perform complicated chemical transformations with high selectivity and efficiency. Through a combination of multi-electron transfer systems, substrate binding sites/channels, and networks of non-covalent interactions, these natural assemblies carry out reactions ranging from high turn-over oxidations/reductions of small molecules (H2, N2, CH4, etc…) to selective multiple stereocenter forming cascade reactions. From a purely synthetic stand point the same reactions can be done in a lab, but often proceed with low efficiency or require long multi-step syntheses. This is to say that, while advances in synthetic chemistry have significantly narrowed the gap between the lab and nature, methods to mimic the reactivity of enzymes remain a valuable goal.
Research in the Singleton group seeks to explore the vast chemical space between small molecule catalysts and machinery of nature. In doing so, our goal is to develop intermediate systems that combine the best aspects of synthetic and natural catalysts. Current projects in the group are focused on:
1) Foldamer scaffolds for mimicking multi-layered coordination environments,
2) Multi-metallic complexes for cooperative catalysis, and
3) Diversely functionalized aromatic receptors for sensing and catalysis.