Date of Award

2014

Document Type

Thesis

Degree Name

Bachelors

Department

Natural Sciences

First Advisor

Sherman, Suzanne

Keywords

Ligands, Blue Copper Proteins, Karlin, Kenneth

Area of Concentration

Chemistry

Abstract

Blue copper proteins are important metalloproteins that are found in plants and bacteria and are involved in photosynthesis, respiration, oxidative deamination of primary amines and reduction of nitrite reductase. They more specifically are involved in reduction and oxidation reactions, mostly as transporters for electrons. They contain at least one type 1 copper center and are characterized by a sulfur to copper charge transfer giving the proteins a blue color. Blue copper proteins generally have a reduction potential between +150 and 800 mV (vs NHE) depending on the coordination sphere. The immediate environment of the copper influences the redox potential of the copper which changes the function of the protein. The structure of the coordination sphere is not determined by the metal cofactor but by the protein itself limiting the preferred geometry of the metal ion. Blue copper proteins are very complex, so researchers synthesize models of the copper centers, mimicking the donor atoms and structure around the copper ion as closely as possible. The initial stage of this project consists of synthesizing the model ligand bis(2-(2-thio-1-methylimidazole) ethyl) amine (L) and forming both the copper (I) and copper (II) complexes, so the structural effects on redox potential can be studied and compared later to other similar complexes. The project was based on and developed from Kenneth Karlin’s work. Three trials of varying ratios of reagents and reaction times were run to determine the best procedure for the model ligand. While the full objective of synthesizing and comparing the copper (I) and copper (II) complexes of the model ligands chosen was not completed, this thesis contains information towards a procedure for the synthesis of the B2T1M ligand.

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