Marcinkeviciene J, Cenas N, Kulys J, Usanov S A, Sukhova N M, Selezneva I S, Gryazev V F
Institute of Biochemistry, Lithuanian Academy of Sciences, Vilnius, Mokslininku, USSR.
Biomed Biochim Acta. 1990;49(4):167-72.
adrenodoxin reductase (E.C. 1.18.1.2) and its complex with adrenodoxin catalyze the aerobic oxidation of NADPH by a number of substituted 2-nitrofurans, 5-nitroimidazoles and p-derivatives of nitrobenzene. The nitrocompounds are reduced via an initial single-electron transfer. Under anaerobic conditions nitrofurans are reduced to the corresponding amines. The rate constants of adrenodoxin oxidation by nitrocompounds vary from 4 x 10(5) to 3 x 10(2) M-1 s-1. A linear correlation between the rate constant logarithm and the single-electron reduction potential at pH 7.0 (E7(1)) of nitrocompounds was observed. The relation between the reactivity and the polarographic half-wave potential (E7(1/2)) is distorted. The reactivity of adrenodoxin reductase is two orders of magnitude lower than that of adrenodoxin.
烟酰胺腺嘌呤二核苷酸磷酸（NADPH）：肾上腺皮质铁氧化还原蛋白还原酶（E.C. 1.18.1.2）及其与肾上腺皮质铁氧化还原蛋白的复合物可催化多种取代的2-硝基呋喃、5-硝基咪唑和硝基苯的对衍生物对NADPH的需氧氧化。硝基化合物通过最初的单电子转移被还原。在厌氧条件下，硝基呋喃被还原为相应的胺。硝基化合物氧化肾上腺皮质铁氧化还原蛋白的速率常数在4×10⁵至3×10²M⁻¹ s⁻¹之间变化。观察到在pH 7.0时，速率常数对数与硝基化合物的单电子还原电位（E7(1)）之间存在线性相关性。反应活性与极谱半波电位（E7(1/2)）之间的关系发生了扭曲。肾上腺皮质铁氧化还原蛋白还原酶的反应活性比肾上腺皮质铁氧化还原蛋白低两个数量级。
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