Abstract
To characterize a diheme cytochrome c 4 of unknown functional of the Vibrio genus for the first time, the Vibrio parahaemolyticus cytochrome c 4 was overexpressed in Escherichia coli periplasm using the endogenous signal sequence. The physicochemical properties of the purified recombinant protein, viz., molecular mass, UV/Vis, and CD spectra, and the redox potentials of the N- and C-terminal domain hemes were determined.