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Direct electrochemistry of cytochrome c on nanotextured diamond surface

: Yang, N.; Hoffmann, R.; Smirnov, W.; Kriele, A.; Nebel, C.E.


Electrochemistry communications 12 (2010), No.9, pp.1218-1221
ISSN: 1388-2481
Journal Article
Fraunhofer IAF ()
cytochrome c; peroxidase activity; nanostructure; diamond electrochemistry

Nanotextured diamond surfaces with geometrical properties close to protein dimensions were used for the realization of direct electron transfer of cytochrome c (cyt c) without any covalent bonding. The peroxidase activity of native and denatured cyt c was also investigated. Cyclic voltammograms of native cyt c show quasi-reversible electron transfer reactions, while no heme redox activity is detected for denatured cyt c. Unfolding (denaturation) of cyt c can be achieved in the presence of hydrogen peroxide. Partially or fully denatured cyt c showed higher peroxidase activity than native cyt c. This is because denatured cyt c loses its tertiary structure and hydrogen peroxide is easier to access the heme redox center. The apparent Michaelis-Menten constant K-m for native and denatured cyt c has been determined to be 0.23 mM and 0.08 mM.