Interface properties of cytochrome c on a nano-textured diamond surface

• Published in: Diamond and related materials Vol. 20; no. 2; pp. 269 - 273
• Main Authors: Yang, Nianjun, Hoffmann, Rene, Smirnov, Waldemar, Nebel, Christoph E.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 01.02.2011; Elsevier
• Subjects: Chemistry; Condensed matter: structure, mechanical and thermal properties; Constants; Cross-disciplinary physics: materials science; rheology; Cytochrome c; Cytochromes; Diamond electrochemistry; Electrochemistry; Electron transfer; Exact sciences and technology; Fullerenes and related materials; diamonds, graphite; General and physical chemistry; Kinetics and mechanism of reactions; Materials science; Nano-structures; Nanocomposites; Nanomaterials; Nanoscale materials and structures: fabrication and characterization; Nanostructure; Other topics in nanoscale materials and structures; Peroxidase; Peroxidase activity; Physics; Solid surfaces and solid-solid interfaces; Specific materials; Surface chemistry; Surfaces and interfaces; thin films and whiskers (structure and nonelectronic properties); Cytochrome c; Diamond electrochemistry; Nano-structures; Peroxidase activity; Hydrogen peroxide; Reversible processes; Macromolecules; Diamonds; Electron transfer; Etching; Nanoparticles; Proteins; Interface properties; Adsorption; Peroxidases; Heme; Electrochemistry; Surface properties; Cytochromes; Nanostructured materials
• ISSN: 0925-9635; 1879-0062
• DOI: 10.1016/j.diamond.2010.12.012

The electron transfer process and the peroxidase activity of native and denatured cytochrome c were investigated on OH-terminated diamond nano-textured surfaces. The nano-textured surfaces with geometrical properties of typical protein dimensions were fabricated by a top-down technology, where diamond nanoparticles are used as etching masks. The cyclic voltammogram of native cytochrome c shows an adsorption-controlled, reversible electron transfer process of the heme redox center, which was not detected for denatured cytochrome c. Native cytochrome c denatures in the presence of hydrogen peroxide. Higher peroxidase activity was found on the denatured cytochrome c than on native cytochrome c. The apparent Michaelis–Menten constants K m for denatured cytochrome c and the native cytochrome c were determined to be 0.08 and 0.23 mM, respectively. ► Cytochrome c was three-dimensionally entrapped on nano-textured diamond surface. ► Direct electron transfer of cytochrome c was realized on diamond nano-textures. ► Higher peroxidase activity was found for denatured cytochrome c than native one.