Date of Award

2019

Document Type

Thesis

Degree Name

Bachelors

Department

Natural Sciences

First Advisor

Sherman, Suzanne

Area of Concentration

Chemistry

Abstract

Synthetic enzyme modeling is an important method in understanding and harnessing biologically complex, catalytic processes. Scorpionate ligands are stable and customizable making them applicable to modeling a wide variety of active sites. One such active site is RuBisCO, a magnesium activated enzyme responsible for carbon fixation in plants. The motivations of creating its model include a possible method for atmospheric carbon dioxide reduction, in addition to a greater understanding of how the enzyme functions. Multiple attempts have been made to synthetically model RuBisCO with scorpionate ligands but have yielded an undesired bis ligand coordination with magnesium. Herein, the attempted synthesis of a novel, oxygen rich ligand, Hbotbia, is described. This ligand is more sterically hindered than scorpionates used in prior models. The aim is that this added hindrance will create the desired 1:1 coordination with magnesium. t-Butyl-(2-nitrophenyl)-amine (16.4% and 29.5% yields) and 1-t-butyl-1,3- benzimidazol-2-one (92.2% and 96.5% yields) were synthesized according to literature procedures.8 Both compounds were one spot by TLC and pure by NMR spectroscopy with some minor solvent impurities. The first novel step involved linking two 1-t-butyl-1,3-benzimidazol-2-one groups using ethyl dichloroacetate, which was attempted by conducting several NMR trials. These trials showed no signs of reactivity. More steps were taken to improve reactivity, including attempts at the Finkelstein reaction. Although Hbotbia has not yet been synthesized, new insights that will inform future work on scorpionate ligand development and halogen substitution were revealed.

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