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CHEMIENERGIZED SPECIES IN PEROXIDASE SYSTEMS
Author(s) -
Cilento Giuseppe,
Durán Nelson,
Zinner Klaus,
Vidigal Carmen C. C.,
Oliveira Olga M. M. Faria,
Haun Marcela,
Fauoni Adelaide,
Augusto Ohara,
Baptista Roberto Casadei de,
Bechara Etelvino J. H.
Publication year - 1978
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.1751-1097.1978.tb06945.x
Subject(s) - phosphorescence , excited state , photochemistry , chemistry , chemiluminescence , singlet state , peroxidase , quenching (fluorescence) , bioluminescence , triplet state , fluorescence , atomic physics , enzyme , physics , organic chemistry , quantum mechanics , biochemistry
— Several hemeprotein‐catalyzed reactions generate products of the type expected from the cleavage of a high energy intermediate. For some systems, the formation, in high yield, of a carbonyl compound in its excited triplet state has been firmly established on the basis of (i) equivalence of the chemiluminescence and phosphorescence spectra of the expected products; (ii) energy transfer to sensitizers containing heavy atoms and (iii) occurrence of photoproducts. The excited species appears to be generated within the enzyme and shielded from quenching by oxygen. It may be quenched, however, via long‐range triplet‐singlet energy transfer. This work strongly supports our hypothesis that excited electronic states are also formed in biological systems which are not necessarily bioluminescent. One of the functions which peroxidases may thus fulfill might be the utilization of the potential of photochemistry in the absence of light.