Theory and Electrochemistry of Cytochrome c
| Autor: | Salman Seyedi, Morteza M. Waskasi, Dmitry V. Matyushov |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
02 engineering and technology
Molecular Dynamics Simulation 010402 general chemistry Electrochemistry 01 natural sciences symbols.namesake Electron transfer Molecular dynamics Stokes shift Materials Chemistry Physical and Theoretical Chemistry Polarization (electrochemistry) Quantum Arrhenius equation biology Chemistry Cytochromes c Active site Electrochemical Techniques 021001 nanoscience & nanotechnology 0104 chemical sciences Surfaces Coatings and Films Chemical physics biology.protein symbols Quantum Theory Thermodynamics Physical chemistry 0210 nano-technology |
| Zdroj: | The Journal of Physical Chemistry B. 121:4958-4967 |
| ISSN: | 1520-5207 1520-6106 |
| DOI: | 10.1021/acs.jpcb.7b00917 |
| Popis: | Extensive simulations of cytochrome c in solution are performed to address the apparent contradiction between large reorganization energies of protein electron transfer typically reported by atomistic simulations and much smaller values produced by protein electrochemistry. The two sets of data are reconciled by deriving the activation barrier for electrochemical reaction in terms of an effective reorganization energy composed of half the Stokes shift (characterizing the medium polarization in response to electron transfer) and the variance reorganization energy (characterizing the breadth of electrostatic fluctuations). This effective reorganization energy is much smaller than each of the two components contributing to it and is fully consistent with electrochemical measurements. Calculations in the range of temperatures between 280 and 360 K combine long, classical molecular dynamics simulations with quantum calculations of the protein active site. The results agree with the Arrhenius plots for the reaction rates and with cyclic voltammetry of cytochrome c immobilized on self-assembled monolayers. Small effective reorganization energy, and the resulting small activation barrier, is a general phenomenology of protein electron transfer allowing fast electron transport within biological energy chains. |
| Databáze: | OpenAIRE |
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