Electrochemistry and electron paramagnetic resonance spectroscopy of cytochrome c and its heme-disrupted analogs

Abstract Cytochrome c (cyt c ) is one of the most studied conjugated proteins due to its electron-transfer properties and ability to regulate the processes involved in homeostasis or apoptosis. Here we report an electrochemical strategy for investigating the electroactivity of cyt c and its analogs with a disrupted heme moiety, i . e . apocytochrome c (acyt c ) and porphyrin cytochrome c (pcyt c ). The electrochemical data are supplemented with low-temperature and spin-probe electron paramagnetic resonance (EPR) spectroscopy. The main contribution of this report is a complex evaluation of cyt c reduction and oxidation at the level of surface-localized amino acid residues and the heme moiety in a single electrochemical scan. The electrochemical pattern of cyt c is substantially different to both analogs acyt c and pcyt c , which could be applicable in further studies on the redox properties and structural stability of cytochromes and other hemeproteins.