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

I. Szilágyi, S. Mikkola, H. Lönnberg, I. Labádi, I. Pálinkó

Research output: Contribution to journalArticle

6 Citations (Scopus)

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-μ-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.

Original languageEnglish
Pages (from-to)1400-1403
Number of pages4
JournalJournal of Inorganic Biochemistry
Volume101
Issue number10
DOIs
Publication statusPublished - Oct 2007

Fingerprint

Dinucleoside Phosphates
Zinc
Copper
Hydrolysis
Messenger RNA
Uridine
Coordination Complexes
Adenosine
Amines
Rate constants
Catalyst activity
Kinetics
Temperature
diadenosine triphosphate
triphosphoric acid

Keywords

  • 5′ cap models
  • ApA
  • ApppA
  • Imidazolate-bridged copper(II)-zinc(II) complex
  • Kinetic measurements
  • Phosphoesterase
  • UpU

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

Cite this

Hydrolysis of dinucleoside phosphates - mRNA 5′ cap analogues - promoted by a binuclear copper(II)-zinc(II) complex. / Szilágyi, I.; Mikkola, S.; Lönnberg, H.; Labádi, I.; Pálinkó, I.

In: Journal of Inorganic Biochemistry, Vol. 101, No. 10, 10.2007, p. 1400-1403.

Research output: Contribution to journalArticle

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