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- W2023974138 abstract "The phosphorescence of tryptophan and proteins was examined in the presence of silver nitrate in order to obtain information on the mechanisms by which Ag+ quenches fluorescence. The 1:1 Ag+-Trp complex is nonfluorescent both at 77 °C and 296 °C and has 3-fold higher phosphorescence quantum yield than the free amino acid. Silver ion causes loss of vibrational structure in the phosphorescence spectrum, and the lifetime decreases from 7.2 to 0.02. These findings are consistent with an intramolecular heavy-atom effect. A nonsulfhydryl protein, trypsinogen, shows changes in phosphorescence which are qualitatively, but not quantitatively, similar to tryptophan in the presence of silver nitrate. Yeast and liver alcohol dehydrogenases have many sulfhydryl groups and show only phosphorescence quenching on addition of Ag+. In this case, quenching occurs by an energy-transfer mechanism. The phosphorescence yield and spectrum of mercuripapain differed from those of papain and were consistent with a heavy atom effect due to Hg2+. The study was technically much facilitated by the use of aqueous snows containing 10% (vv) methanol. Among the advantages of such aqueous snows is the lack of gross denaturation which has in the past been a major objection to protein phosphorescence studies utilizing glasses of organic solvents." @default.
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- W2023974138 title "Phosphorescence of tryptophan and proteins in the presence of silver ion" @default.
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- W2023974138 doi "https://doi.org/10.1016/0003-9861(75)90423-3" @default.
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