Journal
ELIFE
Volume 6, Issue -, Pages -Publisher
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.26933
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Funding
- Deutsche Forschungsgemeinschaft Unifying Concepts in Catalysis, Project E2/E3
- Deutsche Forschungsgemeinschaft [Sonderforschungsbereich 1078]
- National Institutes of Health [GM055302]
- Human Frontier Science Program Project Award [RGP0063/2013 310]
- Biosciences of the Department of Energy [DE-AC02-05CH11231]
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In plants, algae and cyanobacteria, Photosystem II (PSII) catalyzes the light-driven splitting of water at a protein-bound Mn4CaO5-cluster, the water-oxidizing complex (WOC). In the photosynthetic organisms, the light-driven formation of the WOC from dissolved metal ions is a key process because it is essential in both initial activation and continuous repair of PSII. Structural information is required for understanding of this chaperone-free metal-cluster assembly. For the first time, we obtained a structure of PSII from Thermosynechococcus elongatus without the Mn4CaO5-cluster. Surprisingly, cluster-removal leaves the positions of all coordinating amino acid residues and most nearby water molecules largely unaffected, resulting in a pre-organized ligand shell for kinetically competent and error-free photo-assembly of the Mn4CaO5-cluster. First experiments initiating (i) partial disassembly and (ii) partial re-assembly after complete depletion of the Mn4CaO5-cluster agree with a specific bi-manganese cluster, likely a di-mu-oxo bridged pair of Mn(III) ions, as an assembly intermediate.
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