Hydrolysis of dinucleoside phosphates - mRNA 5 ' cap analogues - promoted by a binuclear copper(II)-zinc(II) complex
: Szilagyi I, Mikkola S, Lonnberg H, Labadi I, Palinko I
Publisher: ELSEVIER SCIENCE INC
: 2007
Journal of Inorganic Biochemistry
: JOURNAL OF INORGANIC BIOCHEMISTRY
: J INORG BIOCHEM
: 101
: 10
: 1400
: 1403
: 4
: 0162-0134
DOI: https://doi.org/10.1016/j.jinorgbio.2007.05.017
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.
5' cap models, ApA, ApppA, imidazolate-bridged copper(II)-zinc(II) complex, kinetic measurements, phosphoesterase, UpU