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首页> 外文期刊>Biochemistry >Protein film voltammetry of arsenite oxidase from the chemolithoautotrophic arsenite-oxidizing bacterium NT-26
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Protein film voltammetry of arsenite oxidase from the chemolithoautotrophic arsenite-oxidizing bacterium NT-26

机译：化学自养亚砷酸氧化细菌NT-26中亚砷酸氧化酶的蛋白膜伏安法

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摘要

The chemolithoautotrophic bacterium NT-26 (isolated from a gold mine in the Northern Territory of Australia) is unusual in that it acquires energy by oxidizing arsenite to arsenate while most other arsenic-oxidizing organisms perform this reaction as part of a detoxification mechanism against the potentially harmful arsenite [present as As(OH)3 at neutral pH]. The enzyme that performs this reaction in NT-26 is the molybdoenzyme arsenite oxidase, and it has been previously isolated and characterized. Here we report the direct (unmediated) electrochemistry of NT-26 arsenite oxidase confined to the surface of a pyrolytic graphite working electrode. We have been able to demonstrate that the enzyme functions natively while adsorbed on the electrode where it displays stable and reproducible catalytic electrochemistry in the presence of arsenite. We report a pH dependence of the catalytic electrochemical potential of -33 mV/pH unit that is indicative of proton-coupled electron transfer. We also have performed catalytic voltammetry at a number of temperatures between 5 and 25 degrees C, and the catalytic current (proportional to the turnover number) follows simple Arrhenius behavior.
机译：化能自养细菌NT-26（从澳大利亚北领地的金矿中分离出）是不寻常的，因为它通过氧化亚砷酸盐来获取砷来获取能量，而大多数其他氧化砷的生物体则通过这种反应来作为排毒机制的一部分，以对抗潜在的有害的亚砷酸盐[在中性pH下以As（OH）3的形式存在]。在NT-26中执行此反应的酶是钼酶亚砷酸氧化酶，先前已对其进行了分离和表征。在这里，我们报告了NT-26亚砷氧化酶的直接（未介导的）电化学作用，该化学作用仅限于热解石墨工作电极的表面。我们已经能够证明该酶在吸附到电极上时具有天然功能，在砷存在下，它在电极上显示出稳定且可重现的催化电化学。我们报告了-33 mV / pH单位的催化电化学势的pH依赖性，这表明质子耦合电子转移。我们还在5到25摄氏度之间的许多温度下进行了催化伏安法，并且催化电流（与周转次数成比例）遵循简单的Arrhenius行为。

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