Biology Project Abstract
AN ANALYSIS OF THE REACTION OF CYTOCHROME C PEROXIDASE WITH VARIOUS REACTANTS
Presenter:
Nicholas Kim, Illinois Mathematics and Science Academy, 1500 West Sullivan Road, Aurora, IL 60506; kangho@imsa.edu
Mentor:
Dr. James E. Erman, Department of Chemistry, Northern Illinois University, DeKalb, IL 60115
Abstract:
The purpose of this experiment is to further investigate the structure and function of a heme protein, Cytochrome c Peroxidase (CcP). Amino acid 146 in this protein is thought to control access of negatively charged reactants to the heme group. The hypothesis is that Aspartate 146 on a normal CcP enzyme inhibits reactions with its negative charge. To test this hypothesis, the rates of the reactions between native CcP and a reactant and a mutated, neutral CcP and a reactant will be measured. If the hypothesis is true, then the rate of reaction of para-nitroperoxybenzoate anion should be inhibited less relative to the neutral peroxybenzoic acid in the CcP (D146N) mutant compared to wild-type yeast CcP. The first set of data between the reactions with the mutated CcP and para-nitroperoxybenzoic acid (pNPBA) show less decreased reaction speeds than the reactions with a normal CcP and pNPBA for pH 6-8. These preliminary findings suggest that the hypothesis is true. Unfortunately, only a few pH values have been tested for which does not account for a complete data set.