Version 1
: Received: 12 November 2022 / Approved: 14 November 2022 / Online: 14 November 2022 (02:52:47 CET)
How to cite:
Sarhangi, S. M.; Matyushov, D. V. Electron Tunneling in Biology: When Does it Matter?. Preprints2022, 2022110232. https://doi.org/10.20944/preprints202211.0232.v1
Sarhangi, S. M.; Matyushov, D. V. Electron Tunneling in Biology: When Does it Matter?. Preprints 2022, 2022110232. https://doi.org/10.20944/preprints202211.0232.v1
Sarhangi, S. M.; Matyushov, D. V. Electron Tunneling in Biology: When Does it Matter?. Preprints2022, 2022110232. https://doi.org/10.20944/preprints202211.0232.v1
APA Style
Sarhangi, S. M., & Matyushov, D. V. (2022). Electron Tunneling in Biology: When Does it Matter?. Preprints. https://doi.org/10.20944/preprints202211.0232.v1
Chicago/Turabian Style
Sarhangi, S. M. and Dmitry V. Matyushov. 2022 "Electron Tunneling in Biology: When Does it Matter?" Preprints. https://doi.org/10.20944/preprints202211.0232.v1
Abstract
Electron can tunnel between cofactor molecules positioned along biological electron transport chains up to the distance of ≃20 Å on the millisecond time scale of enzymatic turnover. This tunneling range mostly determines the design of biological energy chains facilitating cross-membrane transport of electrons. Tunneling distance and cofactors’ redox potentials become main physical parameters of this design. The protein identity, flexibility, or dynamics are missing from this picture assigning universal charge-transport properties to all proteins. This paradigm is challenged by dynamical models of electron transfer showing that the hopping rate is constant within the crossover distance R*≃12 Å, followed with an exponential tunneling falloff at longer distances. In this view, energy chains for electron transport are best designed by placing redox cofactors near the crossover distance R*. Protein flexibility and dynamics affect the magnitude of the maximum hopping rate within the crossover radius. Protein charge transport is not driven by universal parameters anymore and protein identity matters.
Keywords
Protein electron transfer; tunneling; protein dynamics; electrowetting; Stokes-shift dy-namics
Subject
Chemistry and Materials Science, Physical Chemistry
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.