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Octaheme nitrite reductase: The mechanism of intramolecular electron transfer and kinetics of nitrite bioelectroreduction
Bioelectrochemistry ( IF 5 ) Pub Date : 2020-11-10 , DOI: 10.1016/j.bioelechem.2020.107699
Victor Andoralov 1 , Sergey Shleev 2 , Natalia Dergousova 3 , Olga Kulikova 3 , Vladimir Popov 4 , Tamara Tikhonova 3
Affiliation  

Detailed impedance and voltammetric studies of hexameric octaheme nitrite reductase immobilized on carbon-based nanomaterials, specifically nanotubes and nanoparticles, were performed. Well-pronounced bioelectrocatalytic reduction of nitrite on enzyme-modified electrodes was obtained. Analysis of the impedance data indicated the absence of long-lived intermediates involved in the nitrite reduction. Cyclic voltammograms of biomodified electrodes had a bi-sigmoidal shape, which pointed to the presence of two enzyme orientations on carbon supports. The maximum (limiting) catalytic currents were determined and, by applying the correction by the mixed kinetics equation, the Tafel dependences were plotted for each catalytic wave/each enzyme orientation. Finally, two schemes for the rate-limiting processes during bioelectrocatalysis were proposed, viz. for low- and high-potential orientations.



中文翻译:

八氢血红素亚硝酸还原酶:分子内电子转移的机理和亚硝酸盐生物电还原的动力学

进行了固定在碳基纳米材料(特别是纳米管和纳米颗粒)上的六聚八氢亚硝酸亚硝酸还原酶的详细阻抗和伏安研究。获得了公认的酶修饰电极上亚硝酸盐的生物电催化还原。阻抗数据分析表明不存在参与亚硝酸盐还原的长寿命中间体。生物修饰电极的循环伏安图具有双S形形状,表明碳载体上存在两种酶方向。确定最大(极限)催化电流,并通过应用混合动力学方程进行修正,绘制出每种催化波/每种酶取向的Tafel依赖性。最后,提出了两种在生物电催化过程中限速过程的方案。

更新日期:2020-11-21
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