Modeling multicopper oxidase active sites using a triazole-substituted 1,3,5-triethylbenzene

CHED 1192

Jeffrey S. Bandar, jsbandar@csbsju.edu, T. Nicholas Jones, tjones@csbsju.edu, and Brian J. Johnson, bjohnson@csbsju.edu. Department of Chemistry, College of St. Benedict/St. John's University, 37 South College Avenue, St. Joseph, MN 56374
Multicopper oxidases, such as ascorbate oxidase, laccase and ceruloplasmin, couple the four electron reduction of oxygen to the oxidation of substrate molecules. All multicopper oxidases contain an unusual triangular array of copper atoms at the active site. By using a triethylbenzene system to provide facial control, we have synthesized ligand 1 containing triazole and pyridine ring systems to model this active site. Ligand 1 reacts with copper(I) to form a stable complex and the complex has been shown to react with oxygen. This work will discuss the characterization data for this complex. Future work will determine the mode of oxygen binding and the outcome of the oxygenation reaction.

 

Undergraduate Research Poster Session: Inorganic Chemistry
2:00 PM-4:00 PM, Monday, April 7, 2008 Morial Convention Center -- Hall A, Poster

Division of Chemical Education

The 235th ACS National Meeting, New Orleans, LA, April 6-10, 2008