Electron Transfer Route between Quinones in Type-II Reaction Centers

In photosynthetic reaction centers from purple bacteria (PbRCs) and photosystem II (PSII), the photoinduced charge separation is terminated by an electron transfer between the primary (QA) and secondary (QB) quinones. Here, we investigate the electron transfer route, calculating the superexchange coupling (HQA-QB) for electron transfer from QA to QB in the protein environment. HQA-QB is significantly larger in PbRC than in PSII. In superexchange electron tunneling, the electron transfer via unoccupied molecular orbitals of the nonheme Fe complex (QA -> Fe -> QB) is pronounced in PbRC, whereas the electron transfer via occupied molecular orbitals (Fe -> QB followed by QA -> Fe) is pronounced in PSII. The significantly large HQA-QB is caused by a water molecule that donates the H-bond to the ligand Glu-M234 in PbRC. The corresponding water molecule is absent in PSII due to the existence of D1-Tyr246. HQA-QB increases in response to the Ser-L223 center dot center dot center dot QB H-bond formation caused by an extension of the H-bond network, which facilitates charge delocalization over the QB site. This explains the observed discrepancy in the QA-to-QB electron transfer between PbRC and PSII, despite their structural similarity.

Automated summary

The study found that there are differences in the electron transfer pathways in photosynthetic reaction centers from purple bacteria and photosystem II, which are attributed to the presence of a water molecule providing a hydrogen bond and differences in the protein environments.