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• W2115421639 startingPage "1275" @default.
• W2115421639 abstract "Hydrogen bonds are key determinants for protein structures and the fine-tuning of active-site properties. For example, they are responsible for the redox potential variability of protein-imbedded chromophores. By applying high-field (94 GHz) Mims-ENDOR spectroscopy on deuterium-exchanged frozen-solution samples and single crystals of photosystem II from Th. elongatus, we identified the hydrogen-bonding partner of the tyrosyl radical D2-Tyr160, YD., directly by the strength and orientation of the deuterium hyperfine coupling as D2-His189, that is, without relying on the disappearance of a hyperfine coupling interaction upon deletion of D2-His189. No indications for additional hydrogen bonds can be found in the spectra, thereby eliminating hypotheses about a water network as hydrogen-binding partner of YD.." @default.
• W2115421639 created "2016-06-24" @default.
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• W2115421639 creator A5045471541 @default.
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• W2115421639 date "2010-04-21" @default.
• W2115421639 modified "2023-10-15" @default.
• W2115421639 title "High-Field 2H-Mims-ENDOR Spectroscopy on PSII Single Crystals: Hydrogen Bonding of YD." @default.
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• W2115421639 doi "https://doi.org/10.1002/cphc.200901019" @default.
• W2115421639 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20391525" @default.
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