Energetics of the Electron Transfer Pathways in the Homodimeric Photosynthetic Reaction Center

Photosynthetic reaction centers from a green sulfur bacterium (GsbRC), the PscA/PscA proteins, and photosystem I (PSI), PsaA/PsaB proteins, share structural similarities. Here, we report the redox potential (Em) values of GsbRC by solving the linear Poisson-Boltzmann equation and considering the protonation states of all titratable sites in the entire GsbRC protein and identify the factors that shift the Em values with respect to PSI. The Em values for one electron reduction of the accessory (A-1) and adjacent (A0) chlorophylls in GsbRC are 100-250 mV higher than those in PSI, whereas the Em values for the Fe4S4 cluster (FX) are at the same level. The PsaA-Trp697/PsaB-Trp677 pair in PSI, which forms the A1-quinone binding site, is replaced with PscA-Arg638 in GsbRC. PsaB-Asp575 in PSI, which is responsible for the Em difference between A1A and A1B quinones in PSI, is absent in GsbRC. These discrepancies also contribute to the upshift in Em(A-1) and Em(A0) in GsbRC with respect to PSI. It seems likely that the upshifted Em for chlorophylls in GsbRC ultimately originates from the characteristics of the electrostatic environment that corresponds to the A1 site of PSI.

Automated summary

This study reports the redox potential values of the photosynthetic reaction center and identifies the factors that cause the differences with photosystem I. The results show that the redox potential values for certain chlorophylls are higher in the green sulfur bacterium than in photosystem I, while the values for the Fe4S4 cluster are similar. These differences are attributed to the presence of alternative and missing proteins in the green sulfur bacterium.