Structural and energetic insights into Mn-to-Fe substitution in the oxygen-evolving complex.

ABSTRACT: Manganese (Mn) serves as the catalytic center for water splitting in photosystem II (PSII), despite the abundance of iron (Fe) on earth. As a first step toward why Mn and not Fe is employed by Nature in the water oxidation catalyst, we investigated the Fe₄CaO₅ cluster in the PSII protein environment using a quantum mechanical/molecular mechanical (QM/MM) approach, assuming an equivalence between Mn(III/IV) and Fe(II/III). Substituting Mn with Fe resulted in the protonation of μ-oxo bridges at sites O2 and O3 by Arg357 and D1-His337, respectively. While the Mn₄CaO₅ cluster exhibits distinct open- and closed-cubane S₂ conformations, the Fe₄CaO₅ cluster lacks this variability due to an equal spin distribution

SUBMITTER: Saito M 

PROVIDER: S-EPMC10382916 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature