Computational and structural investigation of copper dioxygenase model complexes

CHED 1153

Candace Rowell, candace_rowell@ecats.gcsu.edu, Department of Chemistry & Physics, Georgia College & State University, CBX 082, Milledgeville, GA 31061 and Julia K Metzker, julia.metzker@gcsu.edu, Department of Chemistry and Physics, Georgia College & State University, 231 West Hancock Street, CBX 082, Milledgeville, GA 31061.
In nature, heteroaromatic compounds are degraded by bacteria into aliphatic structures by aromatic-ring-hydroxylating dioxygenase proteins. The study of these metalloenzymes has greatly increased in recent years allowing for a greater understanding of the protein structure and the mechanism for degration. Dr. William Lynch of Armstrong Atlantic State University and coworkers have synthesized a flavonol bound model copper complex, which incorporates a biomemetic ligand to represent the histidine residues found in the protein. The recent work by these authors demonstrates that these copper complexes effectively model the structure and reactivity of flavonol bound copper complexes in nature. We are currently investigating the behavior of these model complexes through density functional computational studies. A comparison of the theoretical and crystallographic parameters will be used to determine the structural model and computational method for future investigations.
 

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