Date of Award
2013
Document Type
Thesis
Degree Name
Bachelors
Department
Natural Sciences
First Advisor
Scudder, Paul
Keywords
Biomimetic, Class 3 Copper Proteins, Tyrosinase
Area of Concentration
Natural Sciences
Abstract
Class 3 copper proteins contain a dinuclear copper active site coordinated by three histidines apiece. These active sites bind dioxygen in a characteristic μ-η2:η2 configuration that results in a strongly antiferromagnetically coupled EPR silent dicopper-peroxo core. This active site functions as a respiratory oxygen carrier in arthropods and mollusks and it catalyzes the oxidation of monophenols and ortho-diphenols which results in a plethora of products that cause pigmentation, protect from pathogens, or act as pathogens through various biosynthetic pathways. These proteins are ubiquitous throughout life signifying their importance. This review aims to describe the function of class 3 protein active sites and surrounding residues of import, explain the biological function many of these proteins play, and illustrate ligands that have been synthesized in the context of the implications of their functionality. Finally, a novel ligand is proposed with reactions for its synthesis outlined and a proposed function described.
Recommended Citation
Hayton, Janardana, "A REVIEW OF TYPE 3 COPPER ACTIVE SITES, THE PROTEINS THEY INHABIT, THEIR FUNCTIONS, AND THEIR BIOMIMETIC LIGANDS" (2013). Theses & ETDs. 4794.
https://digitalcommons.ncf.edu/theses_etds/4794