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Wyświetlanie 1-2 z 2
Tytuł:
Reduction of nitroaromatic compounds by NAD(P)H:quinone oxidoreductase (NQO1): the role of electron-accepting potency and structural parameters in the substrate specificity
Autorzy:
Misevičienė, Lina
Anusevičius, Žilvinas
Šarlauskas, Jonas
Čėnas, Narimantas
Powiązania:
https://bibliotekanauki.pl/articles/1041217.pdf
Data publikacji:
2006
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
reduction potential
DT-diaphorase
nitroaromatic compounds
reduction mechanism
explosives
Opis:
We aimed to elucidate the role of electronic and structural parameters of nitroaromatic compounds in their two-electron reduction by NAD(P)H:quinone oxidoreductase (NQO1, DT-diaphorase, EC 1.6.99.2). The multiparameter regression analysis shows that the reactivity of nitroaromatic compounds (n = 38) increases with an increase in their single-electron reduction potential and the torsion angle between nitrogroup(s) and the aromatic ring. The binding efficiency of nitroaromatics in the active center of NQO1 exerted a less evident role in their reactivity. The reduction of nitroaromatics is characterized by more positive entropies of activation than the reduction of quinones. This points to a less efficient electronic coupling of nitroaromatics with the reduced isoalloxazine ring of FAD, and may explain their lower reactivity as compared to quinones. Another important but poorly understood factor enhancing the reactivity of nitroaromatics is their ability to bind at the dicumarol/quinone binding site in the active center of NQO1.
Źródło:
Acta Biochimica Polonica; 2006, 53, 3; 569-576
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Two-electron reduction of quinones by Enterobacter cloacae PB2 pentaerythritol tetranitrate reductase: quantitative structure-activity relationships
Autorzy:
Misevičienė, Lina
Anusevičius, Žilvinas
Šarlauskas, Jonas
Harris, Richard
Scrutton, Nigel
Čėnas, Narimantas
Powiązania:
https://bibliotekanauki.pl/articles/1041091.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
pentaerythritol tetranitrate reductase
reduction mechanism
electron-transfer
quinones
Opis:
In order to clarify the poorly understood mechanisms of two-electron reduction of quinones by flavoenzymes, we examined the quinone reductase reactions of a member of a structurally distinct old yellow enzyme family, Enterobacter cloacae PB2 pentaerythritol tetranitrate reductase (PETNR). PETNR catalyzes two-electron reduction of quinones according to a 'ping-pong' scheme. A multiparameter analysis shows that the reactivity of quinones increases with an increase in their single-electron reduction potential and pKa of their semiquinones (a three-step (e-,H+,e-) hydride transfer scheme), or with an increase in their hydride-transfer potential (E7(H-)) (a single-step (H-) hydride transfer scheme), and decreases with a decrease in their van der Waals volume. However, the pH-dependence of PETNR reactivity is more consistent with a single-step hydride transfer. A comparison of X-ray data of PETNR, mammalian NAD(P)H : quinone oxidoreductase (NQO1), and Enterobacter cloacae nitroreductase, which reduce quinones in a two-electron way, and their reactivity revealed that PETNR is much less reactive, and much less sensitive to the quinone substrate steric effects than NQO1. This may be attributed to the lack of π-π stacking between quinone and the displaced aromatic amino acid in the active center, e.g., with Phe-178' in NQO1.
Źródło:
Acta Biochimica Polonica; 2007, 54, 2; 379-385
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-2 z 2

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