Modeling the structure and function of 3,4-PCD with new amino-alcohol ligands

CHED 1193

Eric Yoon, eyoon08@holycross.edu1, Mark V. Andrews Jr., mvandr07@holycross.edu2, Christine S. Higham, cshigh06@holycross.edu2, Anil Cetin, ac30@uakron.edu3, Christopher J. Ziegler, ziegler@uakron.edu3, and Joshua R. Farrell, jfarrell@holycross.edu2. (1) Chemistry, College of the Holy Cross, 1 College St., Box 2863, Worcester, MA 01610, (2) Department of Chemistry, College of the Holy Cross, 1 College St., Worcester, MA 01610, (3) Department of Chemistry, University of Akron, KNCL 402, Akron, OH 44325
Enzyme activity is a major subject of interest in biochemistry. We are attempting to model the structure and function of metallo-enzymes and proteins using small molecules as models. Mannich condensations were employed to synthesize novel ligands with two different phenol rings with varying steric bulk and electronic environments. These ligands were used in reactions with anhydrous ferric chloride in an air free environment in order to produce a model for the enzyme protocatechuate 3,4-dioxygenase (PCD). Product study of 3,5-di-t-butylcatechol with iron complexes using mass spectroscopy revealed several products of catechol cleavage. Kinetic study of catechol reaction with iron ligand complex and molecular oxygen was done to investigate catechol 1,2-dioxygenase activity of iron (III) complexes.
 

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