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ABSTRACT Temperature Dependence of the Formal Potential and the Rate Constant of the Heterogeneous Electron Transfer Reaction of Myoglobin By Alison Jayne Anderson, M.S. thank you in advance to the following people: http://www.phattimes.com/myoglobin/acknowledgments.htm for your listening enjoyment and open in explorer, visit the PHAT TIMES tunes sound player: need g2player
http://www.real.com A thesis submitted in partial fulfillment of the requirements for the degree of Master of Science at Virginia Commonwealth University. Virginia Commonwealth University, 1999 Major Director: Dr.
Fred M. Hawkridge, Professor, Department of Chemistry The temperature dependence of the formal potential and the rate constant of the heterogeneous electron transfer reaction of myoglobin has been investigated using cyclic voltammetry. Evidence for the non-spontaneous disassociation of the heme from the protein followed by the spontaneous complete unfolding and denaturation of the protein is indicated by a radical change in the reaction center entropy (D Src) at 37° C. Furthermore, from 5-37° C, the cyclic voltammograms display trends consistent with the gradual increase in the reversibility of the reaction. From 37-50° C, the cyclic voltammograms show switch to more irreversible reactions. The electrochemistry of myoglobin will be analyzed and discussed in context with analogous experimental studies which have been performed on ferricyanide and cytochrome c. |