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Electronic structure of the oxygen-evolving complex in photosystem II prior to O-O bond formation

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Cox,  Nicholas
Research Department Lubitz, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Retegan,  Marius
Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Neese,  Frank
Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Pantazis,  Dimitrios A.
Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Lubitz,  Wolfgang
Research Department Lubitz, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Citation

Cox, N., Retegan, M., Neese, F., Pantazis, D. A., Boussac, A., & Lubitz, W. (2014). Electronic structure of the oxygen-evolving complex in photosystem II prior to O-O bond formation. Science, 345(6198), 804-808. doi:10.1126/science.1254910.


Cite as: https://hdl.handle.net/21.11116/0000-0007-43A1-7
Abstract
The photosynthetic protein complex photosystem II oxidizes water to molecular oxygen at an embedded tetramanganese-calcium cluster. Resolving the geometric and electronic structure of this cluster in its highest metastable catalytic state (designated S3) is a prerequisite for understanding the mechanism of O-O bond formation. Here, multifrequency, multidimensional magnetic resonance spectroscopy reveals that all four manganese ions of the catalyst are structurally and electronically similar immediately before the final oxygen evolution step; they all exhibit a 4+ formal oxidation state and octahedral local geometry. Only one structural model derived from quantum chemical modeling is consistent with all magnetic resonance data; its formation requires the binding of an additional water molecule. O-O bond formation would then proceed by the coupling of two proximal manganese-bound oxygens in the transition state of the cofactor.