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TRIPLET STATE STUDIES OF FLAVlNS BY ELECTRON PARAMAGNETIC RESONANCE—II
Author(s) -
Shiga T.,
Piette L.H.
Publication year - 1964
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.1751-1097.1964.tb08778.x
Subject(s) - tryptophan , tyrosine , chemistry , aromatic amino acids , phenylalanine , triplet state , electron paramagnetic resonance , ovalbumin , amino acid , photochemistry , resonance (particle physics) , electron transfer , biochemistry , nuclear magnetic resonance , molecule , organic chemistry , biology , physics , atomic physics , immune system , immunology
— The triplet states of proteins, bovine serum albumin, ovalbumin and d‐amino acid oxidase, were observed by electron paramagnetic resonance at 77°K. The triplet state of aromatic amino acids, tryptophan, tyrosine and phenylalanine was also detected. The protein triplet originates from the tryptophan residues of these proteins. It is suggested that an energy transfer takes place between tyrosine and tryptophan.