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Título: | Bioelectrocatalytic Activity of W-Formate Dehydrogenase Covalently Immobilized on Functionalized Gold and Graphite Electrodes |
Autor: | Álvarez-Malmagro, Julia; Oliveira, Ana R.; Gutiérrez Sánchez, Cristina; Villajos, Beatriz; Pereira, Inês A. C.; Vélez, Marisela CSIC ORCID; Pita, Marcos CSIC ORCID ; López de Lacey, Antonio CSIC ORCID | Palabras clave: | Carbon dioxide reduction Formate dehydrogenase Bioelectrocatalysis Oriented immobilization Metalloenzymes |
Fecha de publicación: | 3-mar-2021 | Editor: | American Chemical Society | Citación: | ACS Applied Materials and Interfaces 2021, 13, 10, 11891–11900 | Resumen: | [EN] 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. | Versión del editor: | https://doi.org/10.1021/acsami.0c21932 | URI: | http://hdl.handle.net/10261/252882 | ISSN: | 1944-8244 | E-ISSN: | 1944-8252 |
Aparece en las colecciones: | (ICP) Artículos |
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