Journal
PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES
Volume 369, Issue 1647, Pages -Publisher
ROYAL SOC
DOI: 10.1098/rstb.2013.0324
Keywords
manganese; oxygen-evolving complex; photosystem II; X-ray crystallography; X-ray emission spectroscopy; X-ray free-electron laser
Categories
Funding
- NIH [GM 55302, P41GM103393, GM095887, GM102520]
- Office of Science, Office of Basic Energy Sciences (OBES), Division of Chemical Sciences, Geosciences, and Biosciences of the Department of Energy (DOE) [DE-AC02-05CH11231]
- LBNL Laboratory Directed Research and Development award (DOE) [DE-AC02-05CH11231]
- Human Frontier Research grant [RGP0063/2013]
- DFG-Cluster of Excellence 'UniCat'
- Alexander von Humboldt Foundation
- Ruth L. Kirschstein National Research Service Award [F32GM100595]
- Solar Fuels Strong Research Environment (Umea University)
- Artificial Leaf Project (K&A Wallenberg Foundation), VR
- Energimyndigheten
- DOE OBES
- [Sfb1078]
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The structure of photosystem II and the catalytic intermediate states of the Mn4CaO5 cluster involved in water oxidation have been studied intensively over the past several years. An understanding of the sequential chemistry of light absorption and the mechanism of water oxidation, however, requires a new approach beyond the conventional steady-state crystallography and X-ray spectroscopy at cryogenic temperatures. In this report, we present the preliminary progress using an X-ray free-electron laser to determine simultaneously the light-induced protein dynamics via crystallography and the local chemistry that occurs at the catalytic centre using X-ray spectroscopy under functional conditions at room temperature.
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