Cytochrome c is an extensively studied protein used in folding and unfolding analysis due to its well-known structure, small size and presence of an internal chromophore. The porphyrin structure within the protein does not fluoresce, but this property can be altered through metal replacement. This study investigates a safer method for demetallation of cytochrome c and production of free-base porphyrin. Traditional methods require the use of anhydrous hydrofluoric acid which is not suitable for undergraduate laboratories. This experiment focused on the modification of existing methods to incorporate a combination of more common and less hazardous acids while maintaining a high yield of the metal-free protein. Free-base cytochrome c and its successive product after insertion of another metal were characterized using UV-Vis spectroscopy. This method could be used as a preliminary step in other undergraduate folding and unfolding studies.

Alternative methods for the demetalation and metal insertion of iron-free cytochrome c for implementation in undergraduate laboratories

2019 Spring National Meeting

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