Bioelectrocatalytic Activity of W-Formate Dehydrogenase Covalently Immobilized on Functionalized Gold and Graphite Electrodes.
Bioelectrocatalytic Activity of W-Formate Dehydrogenase Covalently Immobilized on Functionalized Gold and Graphite Electrodes.
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DOI：
10.1021/acsami.0c21932
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发表时间：
2021-03-17
影响因子：
9.5
通讯作者：
De Lacey AL
中科院分区：
文献类型：
--
作者：
Alvarez-Malmagro J;Oliveira AR;Gutiérrez-Sánchez C;Villajos B;Pereira IAC;Vélez M;Pita M;De Lacey AL
减少二氧化碳等温室气体已成为人类面临的主要挑战，研究甲酸脱氢酶等二氧化碳还原酶的电催化特性对于实现这一目标具有重要意义。在这项工作中，我们研究了普通脱硫弧菌 Hildenborough FdhAB 甲酸脱氢酶与化学修饰的金和低密度石墨电极的共价键合，利用静电相互作用有利于酶的定向固定。电化学测量显示甲酸盐的生物电催化氧化和通过直接电子转移 (DET) 的二氧化碳还原。原子力显微镜和石英晶体微天平表征，以及直接电催化和介导电催化的比较表明，甲酸脱氢酶的致密层通过一些交联聚集体固定在电极表面。此外，通过 DET 进行 CO2 电还原生成甲酸盐的操作稳定性显示，法拉第产率约为 100%。
The decrease of greenhouse gases such as CO2 has become a key challenge for the human kind and the study of the electrocatalytic properties of CO2-reducing enzymes such as formate dehydrogenases is of importance for this goal. In this work, we study the covalent bonding of Desulfovibrio vulgaris Hildenborough FdhAB formate dehydrogenase to chemically modified gold and low-density graphite electrodes, using electrostatic interactions for favoring oriented immobilization of the enzyme. Electrochemical measurements show both bioelectrocatalytic oxidation of formate and reduction of CO2 by direct electron transfer (DET). Atomic force microscopy and quartz crystal microbalance characterization, as well as a comparison of direct and mediated electrocatalysis, suggest that a compact layer of formate dehydrogenase was anchored to the electrode surface with some crosslinked aggregates. Furthermore, the operational stability for CO2 electroreduction to formate by DET is shown with approximately 100% Faradaic yield.
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