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SHULAMIT ARIAN MIRA BENJAMINI JEHUDA FEITELSON GABRIEL STEIN 《Photochemistry and photobiology》1970,12(6):481-487
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 H2 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. 相似文献
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