Modeling the active site of protocatechuate dioxygenase using aminoalcohol ligands prepared from Mannich condensations

CHED 1220

Mark V. Andrews Jr., mvandr07@holycross.edu1, Christine S. Higham, cshigh06@holycross.edu1, Anil Cetin, ac30@uakron.edu2, Christopher J. Ziegler, ziegler@uakron.edu2, and Joshua R. Farrell, jfarrell@holycross.edu1. (1) Department of Chemistry, College of the Holy Cross, 1 College St., Worcester, MA 01610, (2) Department of Chemistry, University of Akron, KNCL 402, Akron, OH 44325
We are attempting to model protocatechuate 3,4-dioxygenase (PCD) which is an Fe(III) containing enzyme responsible for bioremediation of catechol and carbon cycling in the environment. We are using a series of Mannich condensations to prepare a variety of amino-alcohol ligands, each with different steric and electronic properties to serve as amino acid analogs. These ligands have been combined with FeCl3 resulting in five and six-coordinate PCD models. At least one of these models combines the biological five coordinate structure of PCD with functional oxidation chemistry. Synthesis of the ligands and metal complexes will be described. The metal complexes have been characterized with single crystal X-ray diffraction studies and UV-visible spectroscopy. Details of the reactions of the metal complexes with catechol and oxygen will be presented, including the distribution of products as determined by GC-MS.
 

Undergraduate Research Poster Session: Inorganic Chemistry
2:00 PM-4:00 PM, Monday, March 26, 2007 Hyatt Regency Chicago -- Riverside Center, Poster

Division of Chemical Education

The 233rd ACS National Meeting, Chicago, IL, March 25-29, 2007