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. 1973 Dec;70(12 Pt 1-2):3703–3706. doi: 10.1073/pnas.70.12.3703

Triplet-Triplet Energy Transfer in α-Trypsin

C A Ghiron *,†, J W Longworth *, N Ramachandran †
PMCID: PMC427310  PMID: 4521197

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.

Keywords: protein structure, tryptophan phosphorescence, electron-exchange interaction

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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