This research explores pathways of electron transfer in protein cytochrome c and its mutants. By altering certain amino acid sequences suspected to be electron entry sites on the surface of the protein, we are able to gain insight on the behavior of electrons in biological processes involving cytochrome c. One mutant of special interest is RC9-C14A, in which an important electron pathway has been removed. We are curious as to what effect this mutation has on the flow of electrons through the protein. Using electrochemistry, we hope to investigate the nature of RC9-C14A and other mutants of cytochrome c. This process involves immobilizing the protein on an alkanethiol-modified gold bead electrode, and measuring the current that passes through the protein when a certain potential is applied. Presently, we will be measuring the electron transfer rate through RC9-C14A in relation to the length of the alkanethiol chain attached to the gold bead electrode.