INTERACTION BETWEEN TYROSINE AND DIVALENT SULFUR IN FLUORESCENCE QUENCHING AND IN THE PHOTOCHEMISTRY OF RIBONUCLEASE |
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| Authors: | SHULAMIT ARIAN MIRA BENJAMINI JEHUDA FEITELSON GABRIEL STEIN |
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| Institution: | Department of Physical Chemistry, Hebrew University, Jerusalem, Israel |
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| Abstract: | Abstract— –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 O2 inhibits photoinactivation and H2S 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. |
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