[Cyt c]=199 M, 0.05 M NaSO,

I was most fortunate to have Dr. Song-Chen Sun, from Ron Birke’s group at City College of New York, Queens College, join the group as a postdoctoral at the same time that a graduate student, David Reed, was in my group. Dr. Sun brought extensive experience in Surface Enhance Resonance Raman Spectroscopy (SERRS) to my group from work with Birke, and Reed had worked with James Terner, an expert in timeresolved Raman spectroscopy of heme proteins and enzymes, as an undergraduate student. With the collaboration of James Terner, an effort to study the time-resolved structure of the oxidized to reduced and the reverse reaction was mounted. Reed’s work, mentioned above on the voltammetry of cytochrome c at silver [44], provided the foundation for this research thrust. However, in this work spin-state marker bands in the SERRS spectra showed that the heme iron was in a denatured five coordinate, low-spin state. The native heme structure for cytochrome c is six coordinate high-spin. The electrochemically roughened silver surfaces used to enhance the Raman signal apparently denatured the cytochrome c present at the electrode surface. Attempts to reproduce the one report in the literature that has described the native conformation of cytochrome c in both redox states at roughened silver surfaces failed in this group. However, during the course of this work Dave Reed found a new effect as described above-the formation of

cytochrome c oligomers on lyophilization-that remains an underappreciated point in the literature.