Abstract
Electrostatic fluctuations within proteins are critical to their biological activity as carriers in electron transport chains typically requiring a significant number of single-electron hops. This mechanistic requirement poses the question of how a sufficient energetic efficiency is achieved. We present the results of numerical simulations of the statistics of electrostatic fluctuations at the protein/water interface. The statistics of the electrostatic potential fluctuations inside the protein is strongly non-Gaussian at high temperatures, but becomes consistent with the linear/Gaussian response below the temperature of the dynamical transition in proteins. At high temperatures the large, non-Gaussian electrostatic noise allows higher efficiency of electron transport chains which can be magnified by an order of magnitude compared to the predictions of Gaussian models. The appearance of non-Gaussian statistics is traced back to a significant polarization of the protein-water interface which slows its relaxation at lower temperatures and becomes kinetically frozen below the temperature of dynamical transition.
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