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Triplet-Triplet Energy Transfer in α-Trypsin

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

Abstract

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
OAI identifier: oai:pubmedcentral.nih.gov:427310
Provided by: PubMed Central
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