ArticlePhilosophical transactions of the Royal Society of London. Series B, Biological sciences2014
The Mn₄Ca photosynthetic water-oxidation catalyst studied by simultaneous X-ray spectroscopy and crystallography using an X-ray free-electron laser.
Article in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed.
- An analysis of the structural changes of the oxygen evolving complex of Photosystem II in the SBiochimica et biophysica acta. Bioenergetics · 2025Review
- Review of serial femtosecond crystallography including the COVID-19 pandemic impact and future outlook.Structure (London, England : 1993) · 2023Review
- Effects of x-ray free-electron laser pulse intensity on the Mn KStructural dynamics (Melville, N.Y.) · 2021Article
- The birth of a new field.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014Article
- Methods development for diffraction and spectroscopy studies of metalloenzymes at X-ray free-electron lasers.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014Review
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12 authors.
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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.
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