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Wyszukujesz frazę "Nivinskas, Henrikas" wg kryterium: Autor

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    Wyświetlanie 1-3 z 3
    Tytuł:
    Cytotoxicity of anticancer aziridinyl-substituted benzoquinones in primary mice splenocytes
    Autorzy:
    Miliukienė, Valė
    Nivinskas, Henrikas
    Čėnas, Narimantas
    Powiązania:
    https://bibliotekanauki.pl/articles/1039227.pdf
    Data publikacji:
    2014
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    aziridinyl-substituted quinones
    cytotoxicity
    oxidative stress
    Opis:
    The anticancer activity of aziridinyl-quinones is mainly attributed to their NAD(P)H:quinone oxidoreductase 1 (NQO1)-catalyzed two-electron reduction into DNA-alkylating products. However, little is known about their cytotoxicity in primary cells, which may be important in understanding their side effects. We found that the cytotoxicity of aziridinyl-unsubstituted quinones (n = 12) in mice splenocytes with a low amount of NQO1, 4 nmol × mg-1 × min-1, was caused mainly by the oxidative stress. Aziridinyl-benzoquinones (n = 6) including a novel anticancer agent RH1 were more cytotoxic than aziridinyl-unsubstituted ones with the similar redox properties, and their cytotoxicity was not decreased by an inhibitor of NQO1, dicumarol. The possible reasons for their enhanced cytotoxicity are discussed.
    Źródło:
    Acta Biochimica Polonica; 2014, 61, 4; 833-836
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Two-electron reduction of nitroaromatic compounds by Enterobacter cloacae NAD(P)H nitroreductase: Description of quantitative structure-activity relationships.
    Autorzy:
    Nivinskas, Henrikas
    Koder, Ronald
    Anusevièius, Žilvinas
    Šarlauskas, Jonas
    Miller, Anne-Frances
    Čenas, Narimantas
    Powiązania:
    https://bibliotekanauki.pl/articles/1044214.pdf
    Data publikacji:
    2000
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    HMX
    nitroreductase
    explosive
    TNT
    electron transfer
    tetryl
    RDX
    pentryl
    Opis:
    Enterobacter cloacae NAD(P)H:nitroreductase catalyzes the reduction of a series of nitroaromatic compounds with steady-state bimolecular rate constants (kcat/Km) ranging from 104 M-1s-1 to 107 M-1s-1 , and oxidizing 2 moles NADH per mole mononitrocompound. Oxidation of excess NADH by polynitrobenzenes including explosives 2,4,6-trinitrotoluene (TNT) and 2,4,6-trinitrophenyl-N-methylnitramine (tetryl), has been observed as a slower secondary process, accompanied by O2 consumption. This type of 'redox cycling' was not related to reactions of nitroaromatic anion-radicals, but was caused by the autoxidation of relatively stable reaction products. The logs kcat/Km of all the compounds examined exhibited parabolic dependence on their enthalpies of single-electron- or two-electron (hydride) reduction, obtained by quantum mechanical calculations. This type of quantitative structure-activity relationships shows that the reactivity of nitroaromatics towards E. cloacae nitroreductase depends mainly on their hydride accepting properties, but not on their particular structure, and does not exclude the possibility of multistep hydride transfer.
    Źródło:
    Acta Biochimica Polonica; 2000, 47, 4; 941-949
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Single-electron reduction of quinone and nitroaromatic xenobiotics by recombinant rat neuronal nitric oxide synthase
    Autorzy:
    Anusevičius, Žilvinas
    Nivinskas, Henrikas
    Šarlauskas, Jonas
    Sari, Marie-Agnes
    Boucher, Jean-Luc
    Čėnas, Narimantas
    Powiązania:
    https://bibliotekanauki.pl/articles/1039577.pdf
    Data publikacji:
    2013
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    antitumour agents
    nitroaromatic compounds
    electron transfer mechanism
    oxidative stress
    quinones
    Neuronal nitric oxide synthase (nNOS)
    Opis:
    We examined the kinetics of single-electron reduction of a large number of structurally diverse quinones and nitroaromatic compounds, including a number of antitumour and antiparasitic drugs, and nitroaromatic explosives by recombinant rat neuronal nitric oxide synthase (nNOS, EC 1.14.13.39), aiming to characterize the role of nNOS in the oxidative stress-type cytotoxicity of the above compounds. The steady-state second-order rate constants (kcat/Km) of reduction of the quinones and nitroaromatics varied from 102 M-1s-1 to 106 M-1s-1, and increased with an increase in their single-electron reduction potentials (E17). The presence of Ca2+/calmodulin enhanced the reactivity of nNOS. These reactions were consistent with an 'outer sphere' electron-transfer mechanism, considering the FMNH./FMNH2 couple of nNOS as the most reactive reduced enzyme form. An analysis of the reactions of nNOS within the 'outer sphere' electron-transfer mechanism gave the approximate values of the distance of electron transfer, 0.39-0.47 nm, which are consistent with the crystal structure of the reductase domain of nNOS. On the other hand, at low oxygen concentrations ([O2] = 40-50 μM), nNOS performs a net two-electron reduction of quinones and nitroaromatics. This implies that NOS may in part be responsible for the bioreductive alkylation by two-electron reduced forms of antitumour aziridinyl-substituted quinones under a modest hypoxia.
    Źródło:
    Acta Biochimica Polonica; 2013, 60, 2; 217-222
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-3 z 3

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