|کد مقاله||کد نشریه||سال انتشار||مقاله انگلیسی||ترجمه فارسی||نسخه تمام متن|
|1925490||1536380||2012||7 صفحه PDF||سفارش دهید||دانلود رایگان|
Thermotoga maritima peroxiredoxin–nitroreductase hybrid enzyme (Prx–NR) consists of a FMN-containing nitroreductase (NR) domain fused to a peroxiredoxin (Prx) domain. These domains seem to function independently as no electron transfer occurs between them. The reduction of quinones and nitroaromatics by NR proceeded in a two-electron manner, and follows a ‘ping-pong’ scheme with sometimes pronounced inhibition by quinone substrate. The comparison of steady- and presteady-state kinetic data shows that in most cases, the oxidative half-reaction may be rate-limiting in the catalytic cycle of NR. The enzyme was inhibited by dicumarol, a classical inhibitor of oxygen-insensitive nitroreductases. The reduction of quinones and nitroaromatic compounds by Prx–NR was characterized by the linear dependence of their reactivity (log kcat/Km) on their single-electron reduction potentials E71, while the reactivity of quinones markedly exceeded the one with nitroaromatics. It shows that NR lacks the specificity for the particular structure of these oxidants, except their single-electron accepting potency and the rate of electron self-exchange. It points to the possibility of a single-electron transfer step in a net two-electron reduction of quinones and nitroaromatics by T. maritima Prx–NR, and to a significant diversity of the structures of flavoenzymes which may perform the two-electron reduction of quinones and nitroaromatics.
► Thermotoga maritima contains unique peroxiredoxin–nitroreductase protein (Prx–NR).
► Nitroreductase (NR) and peroxiredoxin (Prx) domains of Prx–NR act independently.
► Quinones and nitroaromatic compounds are reduced by NR domain in two-electron way.
► The reactivity of compounds depends on their reduction potential but not structure.
► The structural diversity of oxygen-insensitive nitroreductases is demonstrated.
Journal: Archives of Biochemistry and Biophysics - Volume 528, Issue 1, 1 December 2012, Pages 50–56