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INTRAMOLECULAR TRYPTOPHAN HEME ENERGY TRANSFER IN HORSERADISH PEROXIDASE
Author(s) -
Brunet Juan E.,
Gonzalez Gustavo A.,
Sotomayor Carlos P.
Publication year - 1983
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.1751-1097.1983.tb03871.x
Subject(s) - horseradish peroxidase , heme , chemistry , intramolecular force , photochemistry , phosphorescence , peroxidase , tryptophan , residue (chemistry) , energy transfer , stereochemistry , fluorescence , organic chemistry , biochemistry , enzyme , amino acid , physics , quantum mechanics , molecular physics
— Chain folding of horseradish peroxidase allocates its sole tryptophanyl residue at a distance of 18 A from the active site heme group as determined by electronic energy transfer. This finding confirms that the phosphorescence spectrum observed in the peroxidase catalyzed oxidation of isobutyraldehydc is due to the excited triplet state acetone produced.