Quinone-and nitroreductase reactions of Thermotoga maritima 3 peroxiredoxin–nitroreductase hybrid enzyme

Abstract : 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 E 7^1, 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
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Archives of Biochemistry and Biophysics, Elsevier, 2012, 528 (1), pp.50-56. 〈10.1016/j.abb.2012.08.014〉
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Zilvinas Anusevicius, Lina Misevičienė, Jonas Šarlauskas, Nicolas Rouhier, Jean-Pierre Jacquot, et al.. Quinone-and nitroreductase reactions of Thermotoga maritima 3 peroxiredoxin–nitroreductase hybrid enzyme. Archives of Biochemistry and Biophysics, Elsevier, 2012, 528 (1), pp.50-56. 〈10.1016/j.abb.2012.08.014〉. 〈hal-01332162〉

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