Metal complexes of macrocyclic ligands mimicking enzyme activity

LUBAL, Přemysl, Antonín ŠTĚPÁNEK a Zdeňka JAROLÍMOVÁ. Metal complexes of macrocyclic ligands mimicking enzyme activity. In Abstract Book of ISABC 10 conference (International Symposium on Applied Bioinorganic Chemistry). Debrecen: Department of Inorganic and Analytical Chemistry, Debrecen University, 2009, 224 s. ISBN 978-963-473-307-2.

Základní údaje

• Originální název: Metal complexes of macrocyclic ligands mimicking enzyme activity
• Název česky: Kovové komplexy macrocyklických ligandů jako modely enzymů
• Autoři: LUBAL, Přemysl (203 Česká republika, garant, domácí), Antonín ŠTĚPÁNEK (203 Česká republika, domácí) a Zdeňka JAROLÍMOVÁ (203 Česká republika, domácí).
• Vydání: Debrecen, Abstract Book of ISABC 10 conference (International Symposium on Applied Bioinorganic Chemistry), 224 s. 2009.
• Nakladatel: Department of Inorganic and Analytical Chemistry, Debrecen University

Další údaje

• Originální jazyk: angličtina
• Typ výsledku: Stať ve sborníku
• Obor: 10406 Analytical chemistry
• Stát vydavatele: Maďarsko
• Utajení: není předmětem státního či obchodního tajemství
• Kód RIV: RIV/00216224:14310/09:00037452
• Organizační jednotka: Přírodovědecká fakulta
• ISBN: 978-963-473-307-2
• Klíčová slova anglicky: macrocyclic ligands; metal complexes; enzyme; analytical determination; nucleotides
• Příznaky: Mezinárodní význam

Anotace

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. Thymin, Uracil, Cytosin, Adenin, Guanin, and their simple nucleosides and nucleotides) on rate of ester hydrolysis was studied. The effect of minute structural changes of inhibitors is the highest for nucleotides and the smallest for bases. The inhibition constants were evaluated from experimental data and compared with analogous systems. 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. Thymin, Uracil, Cytosin, Adenin, Guanin, and their simple nucleosides and nucleotides) on rate of ester hydrolysis was studied. The effect of minute structural changes of inhibitors is the highest for nucleotides and the smallest for bases. The inhibition constants were evaluated from experimental data and compared with analogous systems.

Anotace česky

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. Thymin, Uracil, Cytosin, Adenin, Guanin, and their simple nucleosides and nucleotides) on rate of ester hydrolysis was studied. The effect of minute structural changes of inhibitors is the highest for nucleotides and the smallest for bases. The inhibition constants were evaluated from experimental data and compared with analogous systems. 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. Thymin, Uracil, Cytosin, Adenin, Guanin, and their simple nucleosides and nucleotides) on rate of ester hydrolysis was studied. The effect of minute structural changes of inhibitors is the highest for nucleotides and the smallest for bases. The inhibition constants were evaluated from experimental data and compared with analogous systems.

Návaznosti

• LC06035, projekt VaV: Název: Centrum biofyzikální chemie, bioelektrochemie a bioanalýzy. Nové nástroje pro genomiku, proteomiku a biomedicínu.

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Centrum biofyzikální chemie, bioelektrochemie a bioanalýzy. Nové nástroje pro genomiku, proteomiku a biomedicínu

• ME09065, projekt VaV: Název: Výzkum nových detekčních systémů na bázi senzorových polí pro použití ve speciační analýze

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Výzkum nových detekčních systémů na bázi senzorových polí pro použití ve speciační analýze, Program výzkumu a vývoje KONTAKT (ME)