Cytochrome C

The first reports on direct electrochemistry of a redox active protein were

published in 1977 by Hill [49] and Kuwana [50]. They independently reported that
cytochrome c (cyt c) exhibited virtually reversible electrochemistry on gold and tin
doped indium oxide (ITO) electrodes as revealed by cyclic voltammetry,
respectively. Unlike using specific promoters to realize direct electrochemistry of
protein in the earlier studies, recently a novel approach that only employed specific
modifications of the electrode surface without promoters was developed.
49. M.J. Eddowes and H.A.O. Hill, Novel method for the investigation of the electrochemistry of metalloproteins:
cytochrome c. J. Chem. Soc. Chem. Commun. 21, 771–772 (1977).
50. P. Yeh and T. Kuwana, Reversible electrode reaction of cytochrome c. Chem. Lett. 1145–1148 (1977).

In vivo, cyt c transfers an electron from complex III to complex IV, membrane-
bound
components of the mitochondrial electron-transfer chain.

The electrochemical interrogation of cyt c has, however, been hindered because the
redox-active heme center is buried beneath the surface of the protein. This
difficulty has been overcome by the
introduction of modified electrode surfaces, with monolayers able to interact with
both
the heme center and the underlying electrode. Since the direct electron transfer of
cyt c
was first observed in 1977 [49–50],

Whereas the voltammetric response of cytochrome c is quite poor at bare metal

electrodes, most likely due to protein denaturation at the metal
electrode surface leading to extremely slow electron-transfer
kinetics.