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Binuclear Terbium(III) Complex as a Probe for Tyrosine Phosphorylation

✍ Scribed by Hiroki Akiba; Jun Sumaoka; Makoto Komiyama

Publisher
John Wiley and Sons
Year
2010
Tongue
English
Weight
638 KB
Volume
16
Category
Article
ISSN
0947-6539

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✦ Synopsis

Abstract

By using the luminescence from binuclear complexes of Tb^III^ (Tb~2~‐L^1^ and Tb~2~‐L^2^), phosphorylated Tyr residue in peptides was selectively detected in neutral aqueous solutions. Neither the non‐phosphorylated Tyr, pSer, pThr, nor the other phosphate‐containing biomolecules tested affected the luminescence intensity to any notable extent. Upon the binding of the pTyr to these Tb^III^ complexes, the luminescence from the metal ion was notably promoted, as the light energy absorbed by the benzene ring of pTyr is efficiently transferred to the Tb^III^ center. The binding activity of the binuclear Tb^III^ complexes towards pTyr is two orders of magnitude larger than that of the corresponding mononuclear complex. These binuclear complexes were successfully used for real‐time monitoring of enzymatic phosphorylation of a peptide by a tyrosine kinase.

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