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Statements

Subject Item
n2:RIV%2F00216224%3A14310%2F09%3A00037452%21RIV11-MSM-14310___
rdf:type
skos:Concept n18:Vysledek
dcterms:description
Metal ions form with macrocyclic ligands more stable complexes than with analogous acyclic ligands from both thermodynamic and kinetic point of view. These complexes can be studied as suitable models in order to mimic the metaloenzyme activity. In this contribution, the catalytic activity of [M(cyclen)]2+ complexes (M = Zn, Cd, Cu, Ni, cyclen = 1,4,7,10-tetraazacyclodecane, [12]aneN4) which are mimicking enzymes was investigated for hydrolysis of acetic acid esters acting as substrate. The rate of ester hydrolysis was monitored by molecular absorption (for 4-nitrophenylacetate) or luminescence (for 4-methylumbelliferylacetate) spectroscopy and optimal experimental conditions (e.g. temperature, pH, buffer, etc.) were found. The catalytic activity of the most active Zn(II) and Cd(II) metal complexes is inhibited by some compounds due to formation of stable ternary complexes. The influence of various inhibiting agents (mostly base, e.g. Metal ions form with macrocyclic ligands more stable complexes than with analogous acyclic ligands from both thermodynamic and kinetic point of view. These complexes can be studied as suitable models in order to mimic the metaloenzyme activity. In this contribution, the catalytic activity of [M(cyclen)]2+ complexes (M = Zn, Cd, Cu, Ni, cyclen = 1,4,7,10-tetraazacyclodecane, [12]aneN4) which are mimicking enzymes was investigated for hydrolysis of acetic acid esters acting as substrate. The rate of ester hydrolysis was monitored by molecular absorption (for 4-nitrophenylacetate) or luminescence (for 4-methylumbelliferylacetate) spectroscopy and optimal experimental conditions (e.g. temperature, pH, buffer, etc.) were found. The catalytic activity of the most active Zn(II) and Cd(II) metal complexes is inhibited by some compounds due to formation of stable ternary complexes. The influence of various inhibiting agents (mostly base, e.g.
dcterms:title
Metal complexes of macrocyclic ligands mimicking enzyme activity Metal complexes of macrocyclic ligands mimicking enzyme activity
skos:prefLabel
Metal complexes of macrocyclic ligands mimicking enzyme activity Metal complexes of macrocyclic ligands mimicking enzyme activity
skos:notation
RIV/00216224:14310/09:00037452!RIV11-MSM-14310___
n3:aktivita
n15:S n15:P
n3:aktivity
P(LC06035), P(ME09065), S
n3:dodaniDat
n8:2011
n3:domaciTvurceVysledku
n4:2563266 n4:9764569 n4:9007563
n3:druhVysledku
n17:D
n3:duvernostUdaju
n11:S
n3:entitaPredkladatele
n9:predkladatel
n3:idSjednocenehoVysledku
325602
n3:idVysledku
RIV/00216224:14310/09:00037452
n3:jazykVysledku
n19:eng
n3:klicovaSlova
macrocyclic ligands; metal complexes; enzyme; analytical determination; nucleotides
n3:klicoveSlovo
n6:macrocyclic%20ligands n6:metal%20complexes n6:enzyme n6:analytical%20determination n6:nucleotides
n3:kontrolniKodProRIV
[305624E8F48C]
n3:mistoKonaniAkce
Debrecen
n3:mistoVydani
Debrecen
n3:nazevZdroje
Abstract Book of ISABC 10 conference (International Symposium on Applied Bioinorganic Chemistry)
n3:obor
n12:CB
n3:pocetDomacichTvurcuVysledku
3
n3:pocetTvurcuVysledku
3
n3:projekt
n7:LC06035 n7:ME09065
n3:rokUplatneniVysledku
n8:2009
n3:tvurceVysledku
Štěpánek, Antonín Jarolímová, Zdeňka Lubal, Přemysl
n3:typAkce
n20:WRD
n3:zahajeniAkce
2009-01-01+01:00
s:numberOfPages
224
n16:hasPublisher
Department of Inorganic and Analytical Chemistry, Debrecen University
n10:isbn
978-963-473-307-2
n14:organizacniJednotka
14310