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

Szilágyi, István and Mikkola, S. and Lönnberg, H. and Labádi, Imre and Pálinkó, István (2007) Hydrolysis of dinucleoside phosphates - mRNA 5' cap analogues - promoted by a binuclear copper(II)-zinc(II) complex. JOURNAL OF INORGANIC BIOCHEMISTRY, 101 (10). pp. 1400-1403. ISSN 0162-0134

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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.

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