Master of Science (MS)
Enzymes, Nature’s catalysts, facilitate a vast range of reactions under moderateconditions, with ideal selectivity, and with impressive turnover numbers, making their functionality especially difficult to reproduce. Our group aims to make functional enzyme models so as to enable enzyme-like catalytic activity in an easily modified and scalable synthetic system. Initially, we are aiming to mimic two oxygen-activating enzymes with copper-based catalytic cores – dopamine beta monooxygenase and methane monooxygenase – whose oxygenation activity would have potential applications in medicine and gas-to-liquid fuel production, respectively. Given that the proteinaceous environment surrounding the active site of an enzyme is essential to all metalloproteins, we have designed our own enzyme mimic: the metallopolymer. We hypothesize that by adding secondary coordination sphere interactions and steric bulk in the form of an organic polymeric scaffold to a small molecule active site mimic, we can increase the reactivity and selectivity of our catalysts to better match that of the biological enzymes. Towards that aim, we have synthesized two small molecule copper-based complexes and modified their ligand frameworks with vinyl moieties in the backbone. The vinyl moieties will allow the incorporation of these complexes into a polymer via direct copolymerization or thiol-ene click chemistry. Once synthesized, our metallopolymers can be studied as oxidation catalysts for a range of reactions under various conditions. We will compare the reactivity of our metallopolymers with that of the small molecule analogues to determine what effects the polymer scaffold has on reactivity.
Gordon, Lily Y., "Towards the Synthesis and Evaluation of Cu-Containing Metallopolymers as Functional Enzyme Mimics" (2022). Master's Theses. 5263.
Available for download on Monday, August 23, 2027