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INTERACTION BETWEEN TYROSINE AND DIVALENT SULFUR IN FLUORESCENCE QUENCHING AND IN THE PHOTOCHEMISTRY OF RIBONUCLEASE
Author(s) -
ARIAN SHULAMIT,
BENJAMINI MIRA,
FEITELSON JEHUDA,
STEIN GABRIEL
Publication year - 1970
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.1751-1097.1970.tb06080.x
Subject(s) - chemistry , divalent , tyrosine , photochemistry , fluorescence , ribonuclease , sulfur , quenching (fluorescence) , aqueous solution , excited state , electron transfer , biochemistry , organic chemistry , rna , physics , quantum mechanics , nuclear physics , gene
— –Ribonuclease is inactivated in aqueous solution by u.v. light through different mechanisms according to whether divalent sulfur or aromatic amino acids are the primary light absorbers. At 284 nm, absorbed mainly by tyrosine, the presence of O 2 inhibits photoinactivation and H 2 S formation, but does less so at 254 or 313 nm. Based on data with model substances containing disulfide groups a mechanism is indicated in which excited tyrosine is quenched through electron transfer to adjacent divalent sulfur within the protein. Disulfide compounds are shown to be very efficient quenchers of tyrosine fluorescence.