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PHOTOSTATIONARY STATE COMPOSITIONS OF RETINAL and RELATED COMPOUNDS INCLUDED IN ß‐LACTOGLOBULIN. EFFECTS OF PROTEIN HOST ON ISOMER DISTRIBUTION OF POLYENE SUBSTRATES
Author(s) -
Li XiaoYuan,
Liu Robert S. H.
Publication year - 1995
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1995.tb05283.x
Subject(s) - polyene , photostationary state , retinal , chemistry , stereochemistry , biochemistry , biophysics , biology , photoisomerization , isomerization , catalysis
— The UV‐visible absorption spectra and photostationary state compositions of retinal (or the related C‐18 ketone, 3‐dehydroretinal and the C‐22 aldehyde) imbedded in the binding cavity of (3‐lactoglobulin (BLG) are consistent with the view that the carbonyl group of these polyenes are hydrogen‐bonded with the protein host, most likely with the lone protonated lysine residue in the binding pocket. Patterns of variation in photochemical behavior of the imbedded chromophore versus that in solution are discussed in terms of possible specific protein‐substrate interactions. The results are also compared with that of the methyl ether of retinol where similar hydrogen bonding is not possible.