The range of salts used as supporting electrolytes in electrochemical studies of redox
proteins and enzymes varies widely, with the choice of an electrolyte relying on the …

Stable and reversible electrochemical responses of cytochrome c can be measured on bare
unmodified gold and glassy carbon electrodes. It has been found that in phosphate buffers …

The majority of electrochemical studies on metalloproteins have reported the use of
chemically modified electrodes or deliberate use of adsorbed species to obtain persistent …

The redox potential of horse and bovine heart cytochromes c determined through cyclic
voltammetry is exploited to probe for anion–protein interactions, using a Debye–Hückel …

The standard redox potential at I= 0.01, 25° C and pH 7.0 has been determined for the
following species of cytochrome c: horse heart, baker's yeast isoenzyme‐1, Candida species …

The solvent dielectric constant is considered an important factor in determining the redox
potential of the heme-containing protein cytochrome c in solution. In this study, we …

Revised Manuscript Received November 21, 1994® abstract: Redox reactions between
different c-type cytochromes were monitored by stopped-flow spectroscopy. Second-order …

The electrochemical behavior of biologically important heme proteins such as cytochrome c
is currently one of the most attractive research topics in bioelectrochemistry. Recently, rapid …

Membrane (carbon or gold) electrodes constructed from dialysis membranes varying in
cutoff and charge are used to investigate the electrochemical behavior of c-type …

The dc cyclic voltammetry of several redox proteins at thin film ruthenium dioxide electrodes
is described. Quasi-reversible voltammetric responses were obtained for cytochrome c …