Hydrolysis of dinucleoside phosphates - mRNA 5 ' cap analogues - promoted by a binuclear copper(II)-zinc(II) complex - UTU Research Portal

A1 Refereed original research article in a scientific journal

Hydrolysis of dinucleoside phosphates - mRNA 5 ' cap analogues - promoted by a binuclear copper(II)-zinc(II) complex

Authors: Szilagyi I, Mikkola S, Lonnberg H, Labadi I, Palinko I

Publisher: ELSEVIER SCIENCE INC

Publication year: 2007

Journal: Journal of Inorganic Biochemistry

Journal name in source: JOURNAL OF INORGANIC BIOCHEMISTRY

Journal acronym: J INORG BIOCHEM

Volume: 101

Issue: 10

First page : 1400

Last page: 1403

Number of pages: 4

ISSN: 0162-0134

DOI: https://doi.org/10.1016/j.jinorgbio.2007.05.017

Abstract

The hydrolysis of a 5(/) cap analogue, diadenosinyl-5(/),5(/)-triphosphate (ApppA), and two dinucleoside monophosphates: adenylyl(3(/),5(/))adenosine (ApA) and uridylyl(3(/),5(/))uridine (UpU) promoted by an imidazolate-bridged heterobinuclear copper(II)-zinc(II) complex, Cu(II)-diethylenetriamino-mu-imidazolato-Zn(II)- tris(aminoethyl)amine trisperchlorate (denoted as Cu,Zn-complex in the followings) has been investigated. Kinetic measurements were performed in order to explore the effects of pH, the total concentration of the Cu,Zn-complex and temperature on the cleavage rate. The catalytic activity of the Cu,Zn-complex was quantified by pseudo-first-order rate constants obtained in the excess of the cleaving agent. The results show that the Cu,Zn-complex and its deprotonated forms have phosphoesterase activity and with ApppA the metal complex promoted cleavage takes place selectively within the triphosphate bridge. (C) 2007 Elsevier Inc. All riahts reserved.