巯基弧菌醛氧化还原酶的直接电化学研究。

Margarida M Correia dos Santos, Patrícia M P Sousa, M Lurdes S Gonçalves, M João Romão, Isabel Moura, José J G Moura
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引用次数: 16

摘要

本文报道了DgAOR (Desulfovibrio gigas aldehyde oxidoreductase, DgAOR)的直接电化学反应,DgAOR是黄嘌呤氧化酶家族中的一种钼酶,含有三个氧化还原活性辅助因子:两个[2Fe-2S]中心和一个钼胞嘧啶二核苷酸辅助因子。在金和碳(热解石墨和玻璃碳)电极上分析了酶的伏安行为。使用了两种不同的策略:一种是将分子限制在电极表面,另一种是在溶液中使用DgAOR。在所有研究的情况下,电子转移发生了,尽管不同的氧化还原反应负责伏安信号。通过对DgAOR分子表面的伏安响应和结构特性的深入分析,碳电极上的氧化还原反应可以归因于更多暴露的铁簇[2Fe-2S] II的还原,而钼酸盐辅因子的还原发生在金电极上。在醛的存在伏安结果也被报道和讨论。
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Direct electrochemistry of the Desulfovibrio gigas aldehyde oxidoreductase.

This work reports on the direct electrochemistry of the Desulfovibrio gigas aldehyde oxidoreductase (DgAOR), a molybdenum enzyme of the xanthine oxidase family that contains three redox-active cofactors: two [2Fe-2S] centers and a molybdopterin cytosine dinucleotide cofactor. The voltammetric behavior of the enzyme was analyzed at gold and carbon (pyrolytic graphite and glassy carbon) electrodes. Two different strategies were used: one with the molecules confined to the electrode surface and a second with DgAOR in solution. In all of the cases studied, electron transfer took place, although different redox reactions were responsible for the voltammetric signal. From a thorough analysis of the voltammetric responses and the structural properties of the molecular surface of DgAOR, the redox reaction at the carbon electrodes could be assigned to the reduction of the more exposed iron cluster, [2Fe-2S] II, whereas reduction of the molybdopterin cofactor occurs at the gold electrode. Voltammetric results in the presence of aldehydes are also reported and discussed.

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