Dynamical Effects in Protein Electrochemistry

The Journal of Physical Chemistry. B
Dmitry V Matyushov

Abstract

Electrochemical measurements of electron transfer from an electrode to proteins immobilized at protective layers of varying thickness have shown the presence of two characteristic regimes: (i) exponential (tunneling) decay of the rate constant with the distance to the electrode and (ii) a plateau region where the rate is independent of the distance to the electrode. The reaction in the plateau region is viewed as friction-controlled electron transfer, with the rate constant inversely proportional to the medium relaxation time. Fitting the rates to established theories requires medium relaxation times far exceeding common estimates and relaxation times obtained from computer simulations of the Stokes-shift dynamics. There is a significant disconnect between experimental observations and theoretical expectations. This difficulty is resolved here by allowing additional dissipative dynamics consisting of protein's low-frequency oscillations in a soft harmonic potential describing binding of the protein to the substrate. Protein translational motions modulate the electrode-protein electronic coupling, leading to a new time-scale appearing, along with the Stokes-shift relaxation time, in the pre-exponential factor of the rate constan...Continue Reading

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Oct 10, 2020·The Journal of Chemical Physics·Bruno M Aramburu-TrošeljGerald J Meyer
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