Tyrosyl fluorescence in hemocyanin from the scorpion Leirus quinquestriatus

Alexander Klarman*, Nurith Shaklai, Ezra Daniel

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

The fluorescence properties of hemocyanin from the scorpion Leirus quinquestriatus were studied. Emission and excitation spectra were determined for the protein in both its oxygenated and deoxygenated forms. Oxygenation was found to bring about a large blue shift in the position of the fluorescence maximum, in addition to a marked quenching of the fluorescence intensity as noted before for another hemocyanin. An appreciable tyrosyl contribution to the fluorescence of oxyhemocyanin. was inferred from the wavelength dependence of its emission and excitation spectra. No tyrosyl fluorescence could be observed in either apo- or deoxyhemocyanin. It was concluded that the inability to observe tyrosyl emission in deoxyhemocyanin is due to the dominating emission of tryptophan. The implication of the findings to the often noted failure to detect tyrosyl emission in proteins containing both tyrosine and tryptophan is discussed.

Original languageEnglish
Pages (from-to)322-330
Number of pages9
JournalBBA - Protein Structure
Volume490
Issue number2
DOIs
StatePublished - 22 Feb 1977

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