Authors: Grant Barron, Collin Tuttle, Daniel Scott
Mentors: Daniel Scott
Insitution: Utah Valley University
It has been observed that Myoglobin has the ability to catalyze a reduction of peroxides. Because of this capacity for peroxide reduction in the absence of a qualitative aspects that are attributed to conventional peroxidases it has been classified as a "pseudo" peroxidase. However a theory surrounding the kinetics of macromolecules (known as macromolecular rate theory) has been proposed which would make a quantitative analysis of the origin of Myoglobin's catalytic effect possible by examining reaction rates across a variety of temperatures and concentrations. This data would then be fit to an equation which would allow the derivation of a term that is the heat capacity change of the catalyst-substrate complex and the transition state complex, which would indicate a change in the rigidity of the protein's structure corresponding with enzymatic involvement in the catalysis of the reaction. This change in heat capacity would then be compared to a variety of other catalysts, including a "true" peroxidase, an inorganic catalyst, and another pseudo peroxidase (the data for which would be collected with the same procedure as the data for Myoglobin).