Tb3+ luminescence in metal-substituted alkaline phosphatase

Patrizia Cioni, Giovanni B. Strambini, Paolo Degan

Research output: Contribution to journalArticle

Abstract

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
Volume13
Issue number3-4
DOIs
Publication statusPublished - May 15 1992

Fingerprint

phosphatases
luminescence
tryptophan
Phosphatases
Luminescence
Tryptophan
Alkaline Phosphatase
alkaline phosphatase
Metals
metals
proteins
Proteins
Lanthanoid Series Elements
rare earth elements
chelates
Rare earth elements
metal ions
Excited states
Shielding
Metal ions

Keywords

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

ASJC Scopus subject areas

  • Plant Science
  • Bioengineering
  • Physical and Theoretical Chemistry

Cite this

Tb3+ luminescence in metal-substituted alkaline phosphatase. / Cioni, Patrizia; Strambini, Giovanni B.; Degan, Paolo.

In: Journal of Photochemistry and Photobiology B: Biology, Vol. 13, No. 3-4, 15.05.1992, p. 289-294.

Research output: Contribution to journalArticle

Cioni, Patrizia ; Strambini, Giovanni B. ; Degan, Paolo. / Tb3+ luminescence in metal-substituted alkaline phosphatase. In: Journal of Photochemistry and Photobiology B: Biology. 1992 ; Vol. 13, No. 3-4. pp. 289-294.
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