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 language | English |
---|---|
Pages (from-to) | 289-294 |
Number of pages | 6 |
Journal | Journal of Photochemistry and Photobiology B: Biology |
Volume | 13 |
Issue number | 3-4 |
DOIs | |
Publication status | Published - May 15 1992 |
Keywords
- fluorescence lifetime
- singlet-singlet energy transfer.
- Tb luminescence
ASJC Scopus subject areas
- Plant Science
- Bioengineering
- Physical and Theoretical Chemistry