Protonation structure of the closed-cubane conformation of the O₂-evolving complex in photosystem II.

ABSTRACT: In photosystem II (PSII), one-electron oxidation of the most stable state of the oxygen-evolving Mn₄CaO₅ cluster (S₁) leads to the S₂ state formation, Mn1(III)Mn2(IV)Mn3(IV)Mn4(IV) (open-cubane S₂) or Mn1(IV)Mn2(IV)Mn3(IV)Mn4(III) (closed-cubane S₂). In electron paramagnetic resonance (EPR) spectroscopy, the g = 4.1 signal is not observed in cyanobacterial PSII but in plant PSII, whereas the g = 4.8 signal is observed in cyanobacterial PSII and extrinsic-subunit-depleted plant PSII. Here, we investigated the closed-cubane S₂ conformation, a candidate for a higher spin configuration that accounts for g > 4.1 EPR signal, considering all pairwise exchange couplings in the PSII protein environment (i.e. instead of considering only a single exchange coupling between the [Mn₃(CaO₄)] cubane region and the dangling Mn4 site). Only when a ligand water molecule that forms an H-bond with D1-Asp61 (W1) is deprotonated at dangling Mn4(IV), the g = 4.1 EPR spectra can be reproduced using the cyanobacterial PSII crystal structure. The closed-cubane S₂ is less stable than the open-cubane S₂ in cyanobacterial PSII, which may explain why the g = 4.1 EPR signal is absent in cyanobacterial PSII.

SUBMITTER: Saito K 

PROVIDER: S-EPMC9802176 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature