Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 Å

Photosystem II is the site of photosynthetic water oxidation and contains 20 subunits with a total molecular mass of 350 kDa. The structure of photosystem II has been reported at resolutions from 3.8 to 2.9 Å. These resolutions have provided much information on the arrangement of protein subunits and cofactors but are insufficient to reveal the detailed structure of the catalytic centre of water splitting. Here we report the crystal structure of photosystem II at a resolution of 1.9 Å. From our electron density map, we located all of the metal atoms of the Mn4CaO5 cluster, together with all of their ligands. We found that five oxygen atoms served as oxo bridges linking the five metal atoms, and that four water molecules were bound to the Mn4CaO5 cluster; some of them may therefore serve as substrates for dioxygen formation. We identified more than 1,300 water molecules in each photosystem II monomer. Some of them formed extensive hydrogen-bonding networks that may serve as channels for protons, water or oxygen molecules. The determination of the high-resolution structure of photosystem II will allow us to analyse and understand its functions in great detail. Photosystem II (PSII), found in photosynthetic plants, algae and cyanobacteria, is a large multi-subunit enzyme that harnesses light energy to drive a series of electron-transfer reactions that splits water to produce molecular oxygen. Several medium-resolution structures of PSII have been reported, but the catalytic centre composed of a Mn4CaO5 cluster has proved recalcitrant because of structural distortion caused by X-rays during data collection. This obstacle has now been overcome. Umena et al. present the X-ray structure of PSII at 1.9 Å, sufficient for the assignment of protein subunits and the geometric arrangement of the Mn4CaO5 cluster.