Rezumat
CZU 661:543.68
The electrochemical, spectroscopic and microscopic analyses of cytochrome c and its immobilization on bare glassy carbon (GC) and platinum (Pt) electrodes were performed. Cytochrome c interaction was examined by studying cyanide and arsenic as model compounds for these types of behavior. Subtractively normalized interfacial Fourier transform infrared (SNIFTIR) spectroscopy, fluorescence and electrochemical methods, Fourier transform infrared (FTIR) spectroscopy and atomic force microscopy (AFM) were used to characterize the protein in the immobilized state and to confirm that the protein was not denatured upon binding to the pre-treated bare GC and Pt electrodes. The spherical morphology of the immobilized protein, which is typical of native cytochrome c, was observed using AFM. The protein binding was monitored as a decrease in peak currents (by CV) for the immobilized protein. Under analysis was also a decrease in emission intensities by fluorescence in solution, by the FTIR and SNIFTIR spectroscopies. Fluorescence and AFM proved the existence of the binding process between the protein and the analytes. This behavior was confirmed by the FTIR and SNIFTIR spectroscopies, which gave evidence that the binding event took place at the amino acids side chain of the protein.
Keywords: toxicity, cytochrome c, platinum electrode, glassy carbon electrode.