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 |
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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 journal › Article
}
TY - JOUR
T1 - Tb3+ luminescence in metal-substituted alkaline phosphatase
AU - Cioni, Patrizia
AU - Strambini, Giovanni B.
AU - Degan, Paolo
PY - 1992/5/15
Y1 - 1992/5/15
N2 - 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.
AB - 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.
KW - fluorescence lifetime
KW - singlet-singlet energy transfer.
KW - Tb luminescence
UR - http://www.scopus.com/inward/record.url?scp=0026773973&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0026773973&partnerID=8YFLogxK
U2 - 10.1016/1011-1344(92)85068-6
DO - 10.1016/1011-1344(92)85068-6
M3 - Article
AN - SCOPUS:0026773973
VL - 13
SP - 289
EP - 294
JO - Journal of Photochemistry and Photobiology B: Biology
JF - Journal of Photochemistry and Photobiology B: Biology
SN - 1011-1344
IS - 3-4
ER -