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Cover Picture: Visible‐Light‐Induced Photodimerization of a Photoactive Yellow Protein (PYP) Chromophore Model in a Single Crystal (Chem. Eur. J. 25/2013)
Author(s) -
Nath Naba K.,
Manoj Kochunnoonny,
Gâz Andrei Şerban,
Naumov Panče
Publication year - 2013
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201390089
Subject(s) - chromophore , crystallinity , photochemistry , molecule , radical , chemistry , crystal (programming language) , crystal structure , crystallography , organic chemistry , computer science , programming language
The activity of photoreceptor proteins can be reduced by detrimental radical side reactions. The evolution of radicals in a single crystal of a model molecule for the chromophore of the photoactive yellow protein (PYP) is destructive for the integrity of the tightly packed single crystal. “Dilution” of the structure of the chromophore with water molecules helps retain crystallinity during the photoreaction, providing means for direct observation of the photodimerization reaction by X‐ray diffraction. For more details see the Full Paper by P. Naumov et al. on page 8094 ff.