摘要

By employing a gold surface covered with the substituted mercaptopyrimidine 2-thiobarbituric acid (TBA), it was possible to prove the influence of the surface topography (through a fractal approach) and the formation of an H-bond network between the modified surface and the protein. The spontaneous adsorption of a dense monolayer of cytochrome c led to a quasi-reversible redox behavior with a high direct electron transfer rate constant (38 s(-1)), with no measurable electrocatalytic effect. The redox potential for cytochrome c in the adsorbed state has the same value to that reported for the free protein in solution. Our results suggest that TBA-covered electrodes act as a biomimetic platform that mimic the natural environment to study redox proteins without interfering with their natural behavior.

  • 出版日期2015-6