Tb3+ luminescence in metal-substituted alkaline phosphatase

Patrizia Cioni; Giovanni B. Strambini; Paolo Degan

doi:10.1016/1011-1344(92)85068-6

Tb3+ luminescence in metal-substituted alkaline phosphatase

Patrizia Cioni, Giovanni B. Strambini, Paolo Degan

A.O.U. San Martino - IST, Istituto Nazionale Ricerca sul Cancro (GENOVA)

Research output: Contribution to journal › Article

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	https://doi.org/10.1016/1011-1344(92)85068-6
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

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10.1016/1011-1344(92)85068-6

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Cioni, P., Strambini, G. B., & Degan, P. (1992). Tb3+ luminescence in metal-substituted alkaline phosphatase. Journal of Photochemistry and Photobiology B: Biology, 13(3-4), 289-294. https://doi.org/10.1016/1011-1344(92)85068-6

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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.",

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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

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