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

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

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

Kustantaja: ELSEVIER SCIENCE INC

Julkaisuvuosi: 2007

Journal: Journal of Inorganic Biochemistry

Tietokannassa oleva lehden nimi: JOURNAL OF INORGANIC BIOCHEMISTRY

Lehden akronyymi: J INORG BIOCHEM

Vuosikerta: 101

Numero: 10

Aloitussivu: 1400

Lopetussivu: 1403

Sivujen määrä: 4

ISSN: 0162-0134

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

Tiivistelmä

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.