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.

Rights

This bibliographic record is available under the Creative Commons CC0 public domain dedication. The New College of Florida Libraries, as creator of this bibliographic record, has waived all rights to it worldwide under copyright law, including all related and neighboring rights, to the extent allowed by law.

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