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Triplet-Triplet Energy Transfer in α-Trypsin

By C. A. Ghiron, J. W. Longworth and N. Ramachandran


Experiments are reported that demonstrate that light absorbed by ionized tyrosinyl sensitizes the phosphorescence of tryptophanyl residues of native α-trypsin. The sensitization effect is abolished when α-trypsin is unfolded in guanidine hydrochloride. Under the experimental conditions used, the tryptophan phosphorescence could only have been induced by an electron-exchange interaction. These results, therefore, require that there be at least one ionized tyrosinyl-tryptophanyl pair in the native enzyme and that the distance between the two side chains be sufficiently short to permit electron exchange

Topics: Biological Sciences: Biochemistry
Year: 1973
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Provided by: PubMed Central
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