Abstract
The three tryptophan (trp) residues located at positions 126, 138, and 158 in wild-type bacteriophage T4 lysozyme have been investigated by low temperature phosphorescence and ODMR spectroscopy. Assignment of spectral properties to individual trp residues was facilitated by measurements on mutant proteins containing one or two trp→tyr (tyrosine) substitutions. It has been observed that (i) the triplet state energies (ET) of the trp residues lie in the order: ET(126)>ET(158)>ET(138) and (ii) S→S nonradiative energy transfer takes place predominantly from trp 126 to trp 158. Calculated orientation factors in Förster’s equation using crystal structure data support this result, suggesting a specific direction for the S1←S0 transition moment of trp.
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