Surface packing determines the redox potential shift of cytochrome c adsorbed on gold.


Thermodynamic and dynamic properties of iso-1-cytochrome c covalently bound to a bare gold surface are here investigated by large scale atomistic simulations. The reduction potential of the protein for low and high surface concentrations is calculated showing a good agreement with experimental estimates. The origin of the dependence of the reduction potential on the surface concentration is investigated and is demonstrated to stem from the changing polarizability of the environment surrounding the protein, a mechanism reminiscent of crowding effects. Moreover, structural analyses are performed revealing relevant changes induced by the presence of the electrode on the dynamic properties of cytochrome c. In particular, one of the two cavities previously identified on the protein surface [Bortolotti et al. J. Am. Chem. Soc., 2012, 134, 13670], and that reversibly open in cytochrome c freely diffusing in solution, is found to be deformed when the protein is adsorbed on gold. This modification exemplifies a mechanism that potentially leads to changes in the protein properties by surface-induced modification of its dynamical behavior.

DOI: 10.1021/ja505251a

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@article{ZanettiPolzi2014SurfacePD, title={Surface packing determines the redox potential shift of cytochrome c adsorbed on gold.}, author={Laura Zanetti-Polzi and Isabella Daidone and Carlo Augusto Bortolotti and Stefano Corni}, journal={Journal of the American Chemical Society}, year={2014}, volume={136 37}, pages={12929-37} }