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- W3013362489 endingPage "820" @default.
- W3013362489 startingPage "795" @default.
- W3013362489 abstract "The investigation of water oxidation in photosynthesis has remained a central topic in biochemical research for the last few decades due to the importance of this catalytic process for technological applications. Significant progress has been made following the 2011 report of a high-resolution X-ray crystallographic structure resolving the site of catalysis, a protein-bound Mn 4 CaO x complex, which passes through ≥5 intermediate states in the water-splitting cycle. Spectroscopic techniques complemented by quantum chemical calculations aided in understanding the electronic structure of the cofactor in all (detectable) states of the enzymatic process. Together with isotope labeling, these techniques also revealed the binding of the two substrate water molecules to the cluster. These results are described in the context of recent progress using X-ray crystallography with free-electron lasers on these intermediates. The data are instrumental for developing a model for the biological water oxidation cycle." @default.
- W3013362489 created "2020-04-03" @default.
- W3013362489 creator A5008511927 @default.
- W3013362489 creator A5011066148 @default.
- W3013362489 creator A5083711185 @default.
- W3013362489 date "2020-06-20" @default.
- W3013362489 modified "2023-10-12" @default.
- W3013362489 title "Current Understanding of the Mechanism of Water Oxidation in Photosystem II and Its Relation to XFEL Data" @default.
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