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- W2043947026 abstract "In photosystem II (PSII), the redox properties of the non-heme iron complex (Fe complex) are sensitive to the redox state of quinones (QA/B), which may relate to the electron/proton transfer. We calculated the redox potentials for one-electron oxidation of the Fe complex in PSII [Em(Fe)] based on the reference value Em(Fe) = +400 mV at pH 7 in the QA0QB0 state, considering the protein environment in atomic detail and the associated changes in protonation pattern. Our model yields the pH dependence of Em(Fe) with −60 mV/pH as observed in experimental redox titration. We observed significant deprotonation at D1-Glu244 in the hydrophilic loop region upon Fe complex oxidation. The calculated pKa value for D1-Glu244 depends on the Fe complex redox state, yielding a pKa of 7.5 and 5.5 for Fe2+ and Fe3+, respectively. To account for the pH dependence of Em(Fe), a model involving not only D1-Glu244 but also the other titratable residues (five Glu in the D-de loops and six basic residues near the Fe complex) seems to be needed, implying the existence of a network of residues serving as an internal proton reservoir. Reduction of QA/B yields +302 mV and +268 mV for Em(Fe) in the QA-QB0 and QA0QB- states, respectively. Upon formation of the QA0QB- state, D1-His252 becomes protonated. Forming Fe3+QBH2 by a proton-coupled electron transfer process from the initial state Fe2+QB- results in deprotonation of D1-His252. The two EPR signals observed at g = 1.82 and g = 1.9 in the Fe2+QA- state of PSII may be attributed to D1-His252 with variable and fixed protonation, respectively." @default.
- W2043947026 created "2016-06-24" @default.
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- W2043947026 date "2005-10-21" @default.
- W2043947026 modified "2023-09-26" @default.
- W2043947026 title "Oxidation of the Non-Heme Iron Complex in Photosystem II" @default.
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- W2043947026 doi "https://doi.org/10.1021/bi051099v" @default.
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