Inactivation of redox enzymes and the loss enzyme’s material from its adsorbed film on electrode surface are events that have similar outputs when studied under conditions protein-film voltammetry. In current work, we present a series novel theoretical results cyclic staircase voltammetry clearly reveal how to distinguish between these two events. Theoretical model elaborated in this work compr...

Cyclic voltammetry has been applied for the characterization of cross-linked horse heart cytochrome c (HHC) on cysteamine-modified gold electrodes. The cross-linking, i.e. amide bond formation, between the proteins was achieved by using 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC) as coupling reagent. The optimal conditions for the formation of the HHC film were determined by varying th...

The following review explores applications of voltammetric methods for observing reactions of complex metalloproteins. Attention is focused upon the technique of ‘protein-film voltammetry’, in which the protein molecules under investigation are adsorbed on the electrode surface and electrochemically ‘interrogated.’ The experiments address a minuscule sample with high sensitivity, and optimal co...

Square-wave voltammetry of surface redox reactions is considered as an adequate model for a protein-film voltammetric setup. Here we develop a theoretical approach to analyze the effects of temperature on square-wave voltammograms. The performed simulations address the surface redox reactions featuring slow, modest and fast electron transfer. The theoretical calculations show that the temperatu...

Reactions of the [3Fe-4S] cluster and various metallated [M3Fe-4S] adducts co-ordinated in the ferredoxin from the hyperthermophile Pyrococcus furiosus have been studied by protein-film voltammetry, bulk-solution voltammetry, solution kinetics and magnetic CD (MCD). The [3Fe-4S] cluster exhibits two couples, [3Fe-4S]+/0 and [3Fe-4S]0/2-. Film voltammetry is possible over a wide pH range (2-8), ...