Abstract

The adsorption of cytochromes b 5 and c on the surface of gold electrodes, including the surface modified with cysteine, was studied. The quartz crystal microbalance method with parallel dissipation energy measurements, microcontact printing, and atomic-force microscopy were used to show that the special features of the structure and morphology of two-component cytochrome b 5 and c films were determined by the nature of the proteins themselves and the influence of the modifying “sublayer.” The largest changes in the weight of films and dissipation energy were observed in the adsorption of cytochrome b 5 on a cytochrome c film deposited on a cysteine sublayer. Atomic-force microscopy measurements showed that strong interaction between cytochrome c and b 5 molecules on the surface of gold modified with cysteine could be related to the formation of the corresponding protein complex.

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