Mechanism of Na+/K+-Atpase and Mg2+-Atpase Inhibition By Metal Ions and Complexes
Mehanizam inhibicije Na+/K+–ATPaze i Mg2+–ATPaze metalnim jonima i kompleksima
Апстракт
The aim of the study was to give an overview of the mechanism of inhibition of Na+/K+-ATPase and Mg2+-ATPase activity, the enzymes playing a key role in the active transport of monovalent cations (Na+ and K+) across the cell membrane, induced by the ions of some transition (Cu2+, Zn2+, Fe2+, Co2+) and heavy (Hg2+ i Cd2+) metals, ammonium decavanadate and noble metals complexes ([PtCl2DMSO2], [AuCl4](-), [PdCl4](2-), [PdCl(dien)](+), [PdCl(Me(4)dien)](+)). The extensive kinetic analysis was done in order to determine kinetic parameters and the mode of interaction of Na+/K+-ATPase and Mg2+-ATPase and the investigated compounds. In addition, the ability of sulphur-donor ligands (L-cysteine and glulathione), as well as EDTA, to prevent metal ions and complexes induced inhibition of Na+/K+-ATPase activity and to recover enzymatic activity was investigated Finally, development of highly sensitive and selective analytical tools on the basis of the immobilized enzyme is discussed in this paper....
U ovom radu je dat pregled mehanizma interakcije Na+/K+–ATPaze i Mg2+–ATPaze, enzima koji igraju ključnu ulogu u aktivnom transportu katjona kroz ćelijsku membranu, i jona prelaznih metala (Cu2+, Zn2+, Fe2+ i Co2+), jona teških metala (Hg2+ i Cd2+), amonijum-dekavanadata i kompleksa plemenitih metala ([PtCl2DMSO2], [AuCl4]–, [PdCl4]2–, [PdCl(dien)]+, [PdCl(Me4dien)]+). Kinetička analiza je urađena u cilju određivanja kinetičkih parametara i tipa inhibicije enzima ovim jedinjenjima. Takođe je ispitivana sposobnost L-cisteina i glutationa (koji sadrže sumpor) da spreče inhibiciju Na+/K+–ATPaze matalnim jonima i kompleksima plemenitih metala i reaktiviraju aktivnost inhibiranog enzima. Na kraju, razvoj osetljivih i selektivnih analitičkih oruđa na bazi imobilizovane Na+/K+––ATPaze je razmotren.
Кључне речи:
Na+/K+-ATPase / Mg2+-ATPase / Transition and heavy metals / Noble metal complexes / Decavanadate / Inhibition / Kinetic analysis / Prelazni i teški metali / Kompleksi plemenitih metala / Dekavanadat / Inhibicija / Kinetička analizaИзвор:
Hemijska industrija, 2009, 63, 5a, 499-509Финансирање / пројекти:
- Истраживање механизма интеракција биолошки активних једињења са биомолекулима (RS-MESTD-MPN2006-2010-142051)
DOI: 10.2298/HEMIND0905499V
ISSN: 0367-598X; 2217-7426
WoS: 000274674800006
Scopus: 2-s2.0-77953566625
Колекције
Институција/група
VinčaTY - JOUR AU - Vasić, Vesna M. AU - Čolović, Mirjana B. AU - Krstić, Danijela Z. PY - 2009 UR - https://vinar.vin.bg.ac.rs/handle/123456789/3895 AB - The aim of the study was to give an overview of the mechanism of inhibition of Na+/K+-ATPase and Mg2+-ATPase activity, the enzymes playing a key role in the active transport of monovalent cations (Na+ and K+) across the cell membrane, induced by the ions of some transition (Cu2+, Zn2+, Fe2+, Co2+) and heavy (Hg2+ i Cd2+) metals, ammonium decavanadate and noble metals complexes ([PtCl2DMSO2], [AuCl4](-), [PdCl4](2-), [PdCl(dien)](+), [PdCl(Me(4)dien)](+)). The extensive kinetic analysis was done in order to determine kinetic parameters and the mode of interaction of Na+/K+-ATPase and Mg2+-ATPase and the investigated compounds. In addition, the ability of sulphur-donor ligands (L-cysteine and glulathione), as well as EDTA, to prevent metal ions and complexes induced inhibition of Na+/K+-ATPase activity and to recover enzymatic activity was investigated Finally, development of highly sensitive and selective analytical tools on the basis of the immobilized enzyme is discussed in this paper. AB - U ovom radu je dat pregled mehanizma interakcije Na+/K+–ATPaze i Mg2+–ATPaze, enzima koji igraju ključnu ulogu u aktivnom transportu katjona kroz ćelijsku membranu, i jona prelaznih metala (Cu2+, Zn2+, Fe2+ i Co2+), jona teških metala (Hg2+ i Cd2+), amonijum-dekavanadata i kompleksa plemenitih metala ([PtCl2DMSO2], [AuCl4]–, [PdCl4]2–, [PdCl(dien)]+, [PdCl(Me4dien)]+). Kinetička analiza je urađena u cilju određivanja kinetičkih parametara i tipa inhibicije enzima ovim jedinjenjima. Takođe je ispitivana sposobnost L-cisteina i glutationa (koji sadrže sumpor) da spreče inhibiciju Na+/K+–ATPaze matalnim jonima i kompleksima plemenitih metala i reaktiviraju aktivnost inhibiranog enzima. Na kraju, razvoj osetljivih i selektivnih analitičkih oruđa na bazi imobilizovane Na+/K+––ATPaze je razmotren. T2 - Hemijska industrija T1 - Mechanism of Na+/K+-Atpase and Mg2+-Atpase Inhibition By Metal Ions and Complexes T1 - Mehanizam inhibicije Na+/K+–ATPaze i Mg2+–ATPaze metalnim jonima i kompleksima VL - 63 IS - 5a SP - 499 EP - 509 DO - 10.2298/HEMIND0905499V ER -
@article{ author = "Vasić, Vesna M. and Čolović, Mirjana B. and Krstić, Danijela Z.", year = "2009", abstract = "The aim of the study was to give an overview of the mechanism of inhibition of Na+/K+-ATPase and Mg2+-ATPase activity, the enzymes playing a key role in the active transport of monovalent cations (Na+ and K+) across the cell membrane, induced by the ions of some transition (Cu2+, Zn2+, Fe2+, Co2+) and heavy (Hg2+ i Cd2+) metals, ammonium decavanadate and noble metals complexes ([PtCl2DMSO2], [AuCl4](-), [PdCl4](2-), [PdCl(dien)](+), [PdCl(Me(4)dien)](+)). The extensive kinetic analysis was done in order to determine kinetic parameters and the mode of interaction of Na+/K+-ATPase and Mg2+-ATPase and the investigated compounds. In addition, the ability of sulphur-donor ligands (L-cysteine and glulathione), as well as EDTA, to prevent metal ions and complexes induced inhibition of Na+/K+-ATPase activity and to recover enzymatic activity was investigated Finally, development of highly sensitive and selective analytical tools on the basis of the immobilized enzyme is discussed in this paper., U ovom radu je dat pregled mehanizma interakcije Na+/K+–ATPaze i Mg2+–ATPaze, enzima koji igraju ključnu ulogu u aktivnom transportu katjona kroz ćelijsku membranu, i jona prelaznih metala (Cu2+, Zn2+, Fe2+ i Co2+), jona teških metala (Hg2+ i Cd2+), amonijum-dekavanadata i kompleksa plemenitih metala ([PtCl2DMSO2], [AuCl4]–, [PdCl4]2–, [PdCl(dien)]+, [PdCl(Me4dien)]+). Kinetička analiza je urađena u cilju određivanja kinetičkih parametara i tipa inhibicije enzima ovim jedinjenjima. Takođe je ispitivana sposobnost L-cisteina i glutationa (koji sadrže sumpor) da spreče inhibiciju Na+/K+–ATPaze matalnim jonima i kompleksima plemenitih metala i reaktiviraju aktivnost inhibiranog enzima. Na kraju, razvoj osetljivih i selektivnih analitičkih oruđa na bazi imobilizovane Na+/K+––ATPaze je razmotren.", journal = "Hemijska industrija", title = "Mechanism of Na+/K+-Atpase and Mg2+-Atpase Inhibition By Metal Ions and Complexes, Mehanizam inhibicije Na+/K+–ATPaze i Mg2+–ATPaze metalnim jonima i kompleksima", volume = "63", number = "5a", pages = "499-509", doi = "10.2298/HEMIND0905499V" }
Vasić, V. M., Čolović, M. B.,& Krstić, D. Z.. (2009). Mechanism of Na+/K+-Atpase and Mg2+-Atpase Inhibition By Metal Ions and Complexes. in Hemijska industrija, 63(5a), 499-509. https://doi.org/10.2298/HEMIND0905499V
Vasić VM, Čolović MB, Krstić DZ. Mechanism of Na+/K+-Atpase and Mg2+-Atpase Inhibition By Metal Ions and Complexes. in Hemijska industrija. 2009;63(5a):499-509. doi:10.2298/HEMIND0905499V .
Vasić, Vesna M., Čolović, Mirjana B., Krstić, Danijela Z., "Mechanism of Na+/K+-Atpase and Mg2+-Atpase Inhibition By Metal Ions and Complexes" in Hemijska industrija, 63, no. 5a (2009):499-509, https://doi.org/10.2298/HEMIND0905499V . .