Premium
High‐Field 2 H‐Mims‐ENDOR Spectroscopy on PSII Single Crystals: Hydrogen Bonding of Y D .
Author(s) -
Keßen Sven,
Teutloff Christian,
Kern Jan,
Zouni Athina,
Bittl Robert
Publication year - 2010
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.200901019
Subject(s) - spectroscopy , hydrogen bond , electron paramagnetic resonance spectroscopy , materials science , field (mathematics) , chemistry , crystallography , photochemistry , hydrogen , electron paramagnetic resonance , nuclear magnetic resonance , molecule , physics , organic chemistry , quantum mechanics , mathematics , pure mathematics
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, Y D . , 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 Y D . .