Photosynthetic Reaction Center: A Nonergodic, Dynamically Anisotropic, and Nonlinear Charge-Transport Engine

We ask the question of what is special about photosynthetic reaction center proteins as media for transporting electrons across the lipid membrane. Ergodicity is broken down for the statistics of electrostatic fluctuations in the heliobacterial reaction center studied here by atomistic simulations. It is not restored on the simulation time scale of ∼1 μs, and it allows low activation barriers for electron hops. The medium dynamics are highly anisotropic (depending on the oxidation state) at cofactor sites, allowing a unidirectional flow of charge. This nonlinear protein response to altering the oxidation state combines with the coupling of cofactor polarizabilities to strong intraprotein electric fields to produce nonparabolic and nonergodic free-energy surfaces of electron transfer, allowing low-barrier charge conductivity in proteins.

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Publication Details

Journal
The Journal of Physical Chemistry Letters
Published
2025-10-09
DOI
https://doi.org/10.1021/acs.jpclett.5c02166
Primary Topic
Photosynthetic Processes and Mechanisms
Type
article
Field-Weighted Citation Impact
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article

Photosynthetic Reaction Center: A Nonergodic, Dynamically Anisotropic, and Nonlinear Charge-Transport Engine

Dmitry V. Matyushov, Mohammad Mehdi Pirnia
The Journal of Physical Chemistry Letters
Photosynthetic Processes and Mechanisms
article

Photosynthetic Reaction Center: A Nonergodic, Dynamically Anisotropic, and Nonlinear Charge-Transport Engine

Dmitry V. Matyushov, Mohammad Mehdi Pirnia
article en

Abstract

We ask the question of what is special about photosynthetic reaction center proteins as media for transporting electrons across the lipid membrane. Ergodicity is broken down for the statistics of electrostatic fluctuations in the heliobacterial reaction center studied here by atomistic simulations. It is not restored on the simulation time scale of ∼1 μs, and it allows low activation barriers for electron hops. The medium dynamics are highly anisotropic (depending on the oxidation state) at cofactor sites, allowing a unidirectional flow of charge. This nonlinear protein response to altering the oxidation state combines with the coupling of cofactor polarizabilities to strong intraprotein electric fields to produce nonparabolic and nonergodic free-energy surfaces of electron transfer, allowing low-barrier charge conductivity in proteins.

The Journal of Physical Chemistry LettersVol. 16(41)
Centre of Excellence in Molecular Biology (PK), Arizona State University (US)
Openalex Percentile: Top 75%
Photosynthetic Processes and Mechanisms
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