PHOTOCHEMICAL-LIKE BEHAVIOR OF RIBOFLAVIN IN THE DARK PROMOTED BY ENZYME-GENERATED TRIPLET ACETONE
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Date
1988
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Abstract
Triplet acetone obtained enzymically by the isobutyraldehyde/peroxidase/O2 system transfers its energy to the riboflavin, which changes into a decompsition product of lumichrome type and produces aggregates. When ribflavin and trypotphan are added to this system, further products.sbd.formylkynurenine and an adduct between the riboflavin and the tryptophan.sbd.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.