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The role of the conserved residue proline-62 in the redox potential and stability of the protein cytochrome c-551 was investigated using a mutant in which proline-62 was mutated to lysine (P62K). The P62K mutant protein was heterologously expressed in E. coli under anaerobic conditions and purified by freezing, acidification, dialysis, cation exchange and size exclusion chromatography. Experiments to determine the effect of the P62K mutation on protein stability and redox potential are ongoing.