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- W2002132013 abstract "The effects of NO and fluoride on the iron-quinone complex of the acceptor side of Photosystem II (PSII) are examined by X- and Q-band EPR spectroscopy. It is found that the EPR signal of the iron-nitrosyl complex changes upon addition of F-. The change is determined to be due to a superhyperfine interaction between the electronic spin (S = 3/2) and the fluorine nuclear spin (I = 1/2), indicating that both F- and NO are bound to the same nonheme iron. To the best of our knowledge, this is the first report of simultaneous binding of both F- and NO to the same iron of a mononuclear nonheme protein. On the basis of an analysis of the hyperfine interaction, a cis F−Fe−NO coordination is indicated. Upon illumination of (NO, Cl-)- or (NO, F-)-treated PSII membranes at 200 K, new X- and Q-band EPR signals are observed in B1||B and B1⊥B modes. Quantitative simulations of these signals provide an unambiguous assignment to the iron-quinone complex, QA-{FeNO},7 of the acceptor site of PSII. The exchange interaction between the iron-nitrosyl complex (S = 3/2) and the semiquinone QA- radical (S = 1/2) is determined to be J = +0.5 cm-1 (F-) and +1.3 cm-1 (Cl-) for Hex = JS1S2. A distribution in the exchange coupling is required to satisfactorily simulate the EPR spectra. This distribution is correlated to small structural variations of the iron-quinone acceptor side of PSII." @default.
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- W2002132013 date "1999-09-22" @default.
- W2002132013 modified "2023-10-01" @default.
- W2002132013 title "Simultaneous Binding of Fluoride and NO to the Nonheme Iron of Photosystem II: Quantitative EPR Evidence for a Weak Exchange Interaction between the Semiquinone Q<sub>A</sub><sup>-</sup>and the Iron-Nitrosyl Complex" @default.
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- W2002132013 doi "https://doi.org/10.1021/ja990533b" @default.
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