Pregled bibliografske jedinice broj: 929304
Electrochemical Investigation of the Influence of K2[B3O3F4OH] on the Activity of Immobilized Superoxide Dismutase
Electrochemical Investigation of the Influence of K2[B3O3F4OH] on the Activity of Immobilized Superoxide Dismutase // International Journal of Electrochemical Science, 13 (2018), 3279-3287 doi:10.20964/2018.04.35 (međunarodna recenzija, članak, znanstveni)
CROSBI ID: 929304 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Electrochemical Investigation of the Influence of K2[B3O3F4OH] on the Activity of Immobilized Superoxide Dismutase
Autori
Herenda, Safija ; Ostojić, Jelena ; Hasković, Edhem ; Hasković, Denis, Miloš, Mladen ; Galić, Borivoj
Izvornik
International Journal of Electrochemical Science (1452-3981) 13
(2018);
3279-3287
Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni
Ključne riječi
Oxidoreductase, enzyme kinetics, boroxine derivative, cyclic voltammetry, chronoamperometry
Sažetak
It is known that oxidoreductase is responsible for the regulation of oxidative stress in organisms, and pathological changes occur within the cell in the form of accumulation or lack of superoxide and peroxide radicals if the oxidoreductase activity is disturbed. Currently, the development of drugs that target the affected cells while leaving healthy cells unaffected is of great interest. The action of potential drugs is based on the inhibition / activation of oxidoreductase. In this work, we studied the electrochemical parameters of superoxide dismutase as well as the action of the potential drug of boroxine - dipotassium trioxohydroxytetrafluorotriborate (K2[B3O3F4OH]) as a target therapeutic for enzyme activity. Electrochemical tests were carried out in a classical three-electrode system using cyclic voltammetry and chronoamperometry techniques, and the obtained results were presented in the form of the kinetic parameters with the maximum value of the current obtained when the solution was saturated with the substrate (Imax) and the Michaelis-Menten constant (Km). K2[B3O3F4OH] was proven to be a reversible inhibitor, and the obtained Imax without inhibitor value of 0.014 mM and Km = 12.09 mM. The results from the Lineweaver - Burk diagram show that the inhibition is a partial noncompetitive inhibition type.
Izvorni jezik
Engleski
Znanstvena područja
Kemija
POVEZANOST RADA
Projekti:
HRZZ-IP-2014-09-6897 - Istraživanje bioaktivnih spojeva iz dalmatinskog bilja: njihov antioksidacijski karakter i utjecaj na enzimsku inhibiciju i zdravlje (BioActCom) (Miloš, Mladen, HRZZ - 2014-09) ( CroRIS)
Ustanove:
Kemijsko-tehnološki fakultet, Split
Profili:
Mladen Miloš
(autor)
Citiraj ovu publikaciju:
Časopis indeksira:
- Current Contents Connect (CCC)
- Web of Science Core Collection (WoSCC)
- Science Citation Index Expanded (SCI-EXP)
- SCI-EXP, SSCI i/ili A&HCI
- Scopus