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Protein Medium Facilitates Electron Transfer in Photosynthetic Heliobacterial Reaction Center. | LitMetric

Protein Medium Facilitates Electron Transfer in Photosynthetic Heliobacterial Reaction Center.

J Phys Chem B

School of Molecular Sciences and Department of Physics, Arizona State University, PO Box 871504, Tempe, Arizona 85287-1504, United States.

Published: October 2024

This computational study addresses the question of how large membrane-bound proteins of electron transport chains facilitate fast vector-based charge transport. We study electron transfer reactions following ultrafast initial charge separation induced by absorption of light by P primary pair and leading to the electron localization at the A cofactor. Two subsequent, much slower reactions, electron transfer to the iron-sulfur cluster F and reduction of the menaquinone (MQ) cofactor, are studied by combining molecular dynamics simulations, electronic structure calculations, and theoretical modeling. The low value of the electronic coupling between A and F brings this reaction to the microsecond time scale even at the zero activation barrier. In contrast, A-MQ electron transfer occurs on a subnanosecond time scale and might become the preferred route for charge transport. We elucidate mechanistic properties of the protein medium allowing fast, vectorial charge transfer. The electric field is high and inhomogeneous inside the protein and is coupled to high polarizabilities of cofactors to significantly lower the reaction barrier. The A-MQ separation puts this reaction at the edge between the plateau characterizing the reaction dynamical control and exponential falloff due to electronic tunneling. A strong separation in relaxation times of the medium dynamics for the forward and backward reactions promotes vectorial charge transfer.

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Source
http://dx.doi.org/10.1021/acs.jpcb.4c04956DOI Listing

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