A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
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
Lehti:: 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.
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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