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.
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.
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