If I understand what you did, the first band was ferritin and the second band was cytochrome c. How dark the band of cytochrome c is depends upon its concentration, as one can appreciate from Beer's law. However, the second issue is pH. At neutral pH cytochrome c has an intense red color that is not very different from the color of hemoglobin or myoglobin. If you initially prepared the protein mixture at neutral pH and applied it to the column, you should have seen the red color. The chromatography would have had two effects potentially. One is that the final concentration of the protein changed relative to its starting concentration, and the other is pH. Once the pH was increased, it is possible that a side-chain in close proximity to the heme group was deprotonated (there is one candidate that comes to mind--look up the groups that coordinate to the iron) and that this deprotonation altered the spectrum in some way.