Protein dynamics and electron transfer: electronic decoherence and non-Condon effects
| Autor: | Skourtis, Spiros S., Balabin, I. A., Kawatsu, T., Beratan, David N. |
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| Přispěvatelé: | Skourtis, Spiros S. [0000-0002-5834-248X] |
| Rok vydání: | 2005 |
| Předmět: |
Models
Molecular Quantum decoherence Correlation functions solvent Molecular physics azurin Electron Transport Electron transfer Computational chemistry Azurin correlation function electron transport Coupling pathways chemical bond Redox reactions Quantum tunnelling energy transfer Multidisciplinary Valence (chemistry) Franck-Condon breakdown Chemistry Protein dynamics Autocorrelation article temperature structure analysis molecular dynamics Bond length priority journal Physical Sciences Dephasing protein signal transduction |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America Proc.Natl.Acad.Sci.U.S.A. |
| ISSN: | 0027-8424 |
| Popis: | We compute the autocorrelation function of the donor-acceptor tunneling matrix element 〈 T DA ( t ) T DA (0)〉 for six Ru-azurin derivatives. Comparison of this decay time to the decay time of the time-dependent Franck-Condon factor {computed by Rossky and coworkers [Lockwood, D. M., Cheng, Y.-K. & Rossky, P. J. (2001) Chem. Phys. Lett. 345, 159-165]} reveals the extent to which non-Condon effects influence the electron-transfer rate. 〈 T DA ( t ) T DA (0)〉 is studied as a function of donor-acceptor distance, tunneling pathway structure, tunneling energy, and temperature to explore the structural and dynamical origins of non-Condon effects. For azurin, the correlation function is remarkably insensitive to tunneling pathway structure. The decay time is only slightly shorter than it is for solvent-mediated electron transfer in small organic molecules and originates, largely, from fluctuations of valence angles rather than bond lengths. |
| Databáze: | OpenAIRE |
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