The Mn4Ca photosynthetic water-oxidation catalyst studied by simultaneous X-ray spectroscopy and crystallography using an X-ray free-electron laser. Tran, R., Kern, J., Hattne, J., Koroidov, S., Hellmich, J., Alonso-Mori, R., Sauter, N. K., Bergmann, U., Messinger, J., Zouni, A., Yano, J., & Yachandra, V. K. Philosophical Transactions of the Royal Society B: Biological Sciences, 369(1647):20130324, July, 2014. Publisher: Royal SocietyPaper doi abstract bibtex 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.
@article{tran_mn4ca_2014,
title = {The {Mn4Ca} photosynthetic water-oxidation catalyst studied by simultaneous {X}-ray spectroscopy and crystallography using an {X}-ray free-electron laser},
volume = {369},
url = {https://royalsocietypublishing.org/doi/10.1098/rstb.2013.0324},
doi = {10.1098/rstb.2013.0324},
abstract = {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.},
number = {1647},
urldate = {2024-12-10},
journal = {Philosophical Transactions of the Royal Society B: Biological Sciences},
author = {Tran, Rosalie and Kern, Jan and Hattne, Johan and Koroidov, Sergey and Hellmich, Julia and Alonso-Mori, Roberto and Sauter, Nicholas K. and Bergmann, Uwe and Messinger, Johannes and Zouni, Athina and Yano, Junko and Yachandra, Vittal K.},
month = jul,
year = {2014},
note = {Publisher: Royal Society},
keywords = {X-ray crystallography, X-ray emission spectroscopy, X-ray free-electron laser, manganese, oxygen-evolving complex, photosystem II},
pages = {20130324},
}
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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. 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