Tb3+ luminescence in metal-substituted alkaline phosphatase

Patrizia Cioni, Giovanni B. Strambini, Paolo Degan

Research output: Contribution to journalArticlepeer-review


Tb3+ was found to bind the highest affinity Zn2+ site in alkaline phosphatase and as evidenced by the phosphorescent properties of tryptophan-109 to restore the holoconformation of the protein. Protein-bound Tb3+ displays an intense long-lived emission having two unusual features: (1) sensitization from the excited singlet state of tryptophan and (2) a lifetime (14 ms) which is five times greater than the longest-lived chelates so far known. The long-lived lanthanide emission is consistent with complete shielding of the metal ion from coordination of solvent molecules.

Original languageEnglish
Pages (from-to)289-294
Number of pages6
JournalJournal of Photochemistry and Photobiology B: Biology
Issue number3-4
Publication statusPublished - May 15 1992


  • fluorescence lifetime
  • singlet-singlet energy transfer.
  • Tb luminescence

ASJC Scopus subject areas

  • Plant Science
  • Bioengineering
  • Physical and Theoretical Chemistry


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