Work

Superexchange Electron Transfer and Protein Matrix in the Charge-Separation Process of Photosynthetic Reaction Centers

Year: 2024

Type: article

Abstract: In type-II reaction centers, such as photosystem II (PSII) and reaction centers from purple bacteria (PbRC), light-induced charge separation involves electron transfer from pheophytin (Pheo D1 ) to quinone (Q A ), occurring near a conserved tryptophan residue (D2-Trp253 in PSII and Trp-M252 in PbRC). This study investigates the route of the Pheo D1 -to-Q A electron transfer, focusing on the superexchange coupling (| H PheoD1···QA |) in the PSII protein environment. | H PheoD1···QA | is significantly larger for the Pheo D1 -to-Q A electron transfer via the unoccupied molecular orbitals of D2-Trp253 ([Trp] •– -like intermediate state, 0.73 meV) compared to direct electron transfer (0.13 meV), suggesting that superexchange is the dominant mechanism in the PSII protein environment. While the overall impact of the protein environment is limited, local interactions, particularly H-bonds, enhance superexchange electron transfer by directly affecting the delocalization of molecular orbitals. The D2-W253F mutation significantly decreases the electron transfer rate. The conservation of D2-Trp253/D1-Phe255 (Trp-M252/Phe-L216 in PbRC) in the two branches appears to differentiate superexchange coupling, contributing to the branches being either active or inactive in electron transfer.

Source: The Journal of Physical Chemistry Letters

DOI: 10.1021/acs.jpclett.4c02232

Authors: Keisuke Saito, Hiroyuki Tamura, Hiroshi Ishikita

Institution: The University of Tokyo

Language: English

Topic: Photosynthetic Processes and Mechanisms

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $4,500

Funders: University of Tokyo, Japan Society for the Promotion of Science, Core Research for Evolutional Science and Technology