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PHOTOCHEMICAL‐LIKE BEHAVIOUR OF RIBOFLAVIN IN THE DARK PROMOTED BY ENZYME‐GENERATED TRIPLET ACETONE
Author(s) -
ROJAS JORGE,
SILVA EDUARDO
Publication year - 1988
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.1751-1097.1988.tb02753.x
Subject(s) - riboflavin , chemistry , adduct , acetone , tryptophan , photochemistry , decomposition , chromatography , organic chemistry , biochemistry , amino acid
— Triplet acetone obtained enzymically by the isobutyraldehyde/peroxidase/O 2 system transfers its energy to the riboflavin, which changes into a decomposition product of lumichrome type and produces aggregates. When riboflavin and tryptophan are added to this system, further products—formylkynurenine and an adduct between the riboflavin and the tryptophan—are formed. The adduct can be separated by gel filtration and ion exchange chromatography and is similar to that prepared by irradiating riboflavin in the presence of tryptophan.