- 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