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• W3039559660 abstract "In photosystem II, water oxidation occurs at the oxygen-evolving complex (OEC). The presence of a hydronium ion (H3O+) was proposed at the Cl– binding site and Ca2+-depleted OEC. Using a quantum mechanical/molecular mechanical approach, we report the stability of H3O+ in the PSII protein environment. Neither release of the proton from ligand water molecule W2 at the OEC nor formation of H3O+ at Cl– is energetically favorable. In contrast, H3O+ can exist at the Ca2+-depleted OEC. Even when H3O+ exists in Ca2+-depleted PSII, the H-bond network of the redox-active tyrosine (TyrZ) remains unaltered, retaining the unusually short low-barrier H-bond with D1-His190, and the redox potential of TyrZ, Em(TyrZ), remains unaltered. These observations explain why the oxidation of the Ca2+-depleted Mn4O5 cluster by TyrZ (i.e., the S2 to S3 transition) is not inhibited at low pH. It seems likely that Ca2+ plays a role in not only (i) maintaining the H-bond network and facilitating TyrZ oxidation [tuning Em(TyrZ)] but also (ii) providing the valence of +2, decreasing the pKa of the ligand molecule (W1), and facilitating the release of the proton from W1 in the S2 to S3 transition together with Cl–." @default.
• W3039559660 created "2020-07-10" @default.
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• W3039559660 date "2020-06-30" @default.
• W3039559660 modified "2023-10-14" @default.
• W3039559660 title "Energetics of Ionized Water Molecules in the H-Bond Network near the Ca²⁺ and Cl^– Binding Sites in Photosystem II" @default.
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• W3039559660 doi "https://doi.org/10.1021/acs.biochem.0c00177" @default.
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• W3039559660 hasPublicationYear "2020" @default.
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