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首页> 外文期刊>The journal of physical chemistry, C. Nanomaterials and interfaces >Probing the Electrocatalytic Oxygen Reduction Reaction Reactivity of immobilized Multicopper Oxidase CueO
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Probing the Electrocatalytic Oxygen Reduction Reaction Reactivity of immobilized Multicopper Oxidase CueO

机译：探讨固定化多铜氧化酶CueO的电催化氧还原反应活性

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摘要

The bioelectrocatalytic (oxygen reduction reaction, ORR) properties of the multicopper oxidase CueO immobilized on gold electrodes were investigated. Macroscopic electrochemical techniques were combined with in situ scanning tunneling microscopy (STM) and surface-enhanced Raman spectroscopy at the ensemble and at the single-molecule level. Self-assembled monolayer of mercaptopropionic acid, cysteamine, and p-aminothiophenol were chosen as redox mediators. The highest ORR activity was observed for the protein attached to amino-terminated adlayers. In situ STM experiments revealed that the presence of oxygen causes distinct structure and electronic changes in the metallic centers of the enzyme, which determine the rate of intramolecular electron transfer and, consequently, affect the rate of electron tunneling through the protein. Complementary Raman spectroscopy experiments provided access for monitoring structural changes in the redox state of the type 1 copper center of the immobilized enzyme during the CueO-catalyzed oxygen reduction cycle. These results unequivocally demonstrate the existence of a direct electronic communication between the electrode substrate and the type 1 copper center.
机译：研究了固定在金电极上的多铜氧化酶CueO的生物电催化（氧还原反应，ORR）性能。宏观电化学技术与原位扫描隧道显微镜（STM）和单分子水平的表面增强拉曼光谱相结合。选择巯基丙酸，半胱胺和对氨基硫酚的自组装单层作为氧化还原介体。对于附着在氨基末端的adlayer上的蛋白，观察到最高的ORR活性。原位STM实验表明，氧的存在会导致酶金属中心的结构和电子发生明显变化，这决定了分子内电子转移的速率，从而影响了通过蛋白质的电子隧穿速率。互补拉曼光谱实验提供了在CueO催化的氧还原循环过程中监测固定化酶1型铜中心氧化还原状态的结构变化的途径。这些结果清楚地证明了电极基板和1型铜中心之间存在直接的电子通讯。

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