Purification of Cytochrome C in Bovine beef heart Introduction In this lab the protein Cytochrome c was partially purified from bovine beef heart. Cytochrome c is part of a group of red or brown heme proteins that all have unique visible-light spectra. There are three different types of respiratory Cytochrome, classified as a, b, or c depending on their peak wave lengths of light absorption.1 In the reduced state Cytochrome c has a distinct heme alpha band at 550 nm. This band was used to determine the concentration of Cytochrome after each step.2 Cytochrome c contains a heme prosthetic group center linked covalently to the protein through a thioester bond. The iron in the heme is coordinated by both a histidine and the sulfur of a methionine residue (Figure 1). Positively charged lysine residues surround the surface of the heme interact with some negatively charged residues on complex to which the cytochrome c binds, when it is receiving or donating an electron.3 Cytochrome c is a mobile electron carrier that transports a single electron at a time from complex III of the el......

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