Our research focuses on new methodology, reaction design, and especially transition-metal catalysis. I am interested in bringing these tools to bear on problems within a variety of fields where sophisticated reaction design has the potential to serve as an enabling tool to produce unique insights into complex, interdisciplinary problems.
We are interested in the design of synthetic methodologies that are simple addition reactions, combining readily available, air- and water-stable, feedstock, chemicals. Typically relying on transition-metal catalysis, these methods aspire to fulfill the goals of “green chemistry,” while at the same time affording new insights into the synthesis of complex molecules. The use of simple, stable precursors ameliorates the problems of functional-group compatibility often faced by synthetic chemists. As such, we are investigating hydrogenative, carbonylative, and related carbon-carbon bond-forming reactions. These reactions allow the investigation of catalyst structure for the design of diastereoselective and enantioselective processes.
Nature uses transition-metal cofactors to perform a variety of enzymatic functions—nitrogen fixation, methane oxidation—that are almost certainly impossible without the aid of metal cofactors. The exquisite selectivity obtained by metalloenzymes is an inspiration to organometallic chemists, and is a tribute to the power of molecular evolution as a means of optimizing enzyme efficiency. Chemists have imitated metalloenzyme active sites in an attempt to better understand enzyme function, but in most cases small-molecule or oligopeptide enzyme mimics cannot compete with the efficiency of the native enzyme. However, a significant limitation for nature is that in an oxidative world where transition metals are scarce, only a few metals (Fe, Mn, Cu, Zn), in limited oxidation states, appear frequently in natural metalloenzymes. As chemists, we intend to merge the power of modular polypeptide “ligand” frameworks with the plethora of unique transition-metal catalysts developed by chemists to develop readily optimizable, wholly new metalloenzymes that display bio-orthogonal reactivity, and function in water on biomolecule substrates. This approach allows us to gain insight into important biochemical problems such as protein-protein interactions.
We are pursuing new ways to produce functional polymers with control over polydispersity, end-group structure, and complex polymer architecture. Methods which allow the synthesis of exciting new electroactive polymers for organic electronics and photovoltaics are important targets of this investigation.
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