Journal
SCIENCE
Volume 303, Issue 5665, Pages 1831-1838Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1093087
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Funding
- NIGMS NIH HHS [F32 GM068304-01, F32 GM068304] Funding Source: Medline
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Photosynthesis uses light energy to drive the oxidation of water at an oxygen-evolving catalytic site within photosystem II ( PSII). We report the structure of PSII of the cyanobacterium Thermosynechococcus elongatus at 3.5 angstrom resolution. We have assigned most of the amino acid residues of this 650-kilodalton dimeric multisubunit complex and refined the structure to reveal its molecular architecture. Consequently, we are able to describe details of the binding sites for cofactors and propose a structure of the oxygen-evolving center (OEC). The data strongly suggest that the OEC contains a cubane-like Mn3CaO4 cluster linked to a fourth Mn by a mono-mu-oxo bridge. The details of the surrounding coordination sphere of the metal cluster and the implications for a possible oxygen-evolving mechanism are discussed.
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