Cargando…

Bioelectrocatalytic Activity of W-Formate Dehydrogenase Covalently Immobilized on Functionalized Gold and Graphite Electrodes

[Image: see text] The decrease of greenhouse gases such as CO(2) has become a key challenge for the human kind and the study of the electrocatalytic properties of CO(2)-reducing enzymes such as formate dehydrogenases is of importance for this goal. In this work, we study the covalent bonding of Desu...

Descripción completa

Detalles Bibliográficos
Autores principales: Alvarez-Malmagro, Julia, Oliveira, Ana R., Gutiérrez-Sánchez, Cristina, Villajos, Beatriz, Pereira, Inês A.C., Vélez, Marisela, Pita, Marcos, De Lacey, Antonio L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2021
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8479727/
https://www.ncbi.nlm.nih.gov/pubmed/33656858
http://dx.doi.org/10.1021/acsami.0c21932
_version_ 1784576320981696512
author Alvarez-Malmagro, Julia
Oliveira, Ana R.
Gutiérrez-Sánchez, Cristina
Villajos, Beatriz
Pereira, Inês A.C.
Vélez, Marisela
Pita, Marcos
De Lacey, Antonio L.
author_facet Alvarez-Malmagro, Julia
Oliveira, Ana R.
Gutiérrez-Sánchez, Cristina
Villajos, Beatriz
Pereira, Inês A.C.
Vélez, Marisela
Pita, Marcos
De Lacey, Antonio L.
author_sort Alvarez-Malmagro, Julia
collection PubMed
description [Image: see text] The decrease of greenhouse gases such as CO(2) has become a key challenge for the human kind and the study of the electrocatalytic properties of CO(2)-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 CO(2) 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 CO(2) electroreduction to formate by DET is shown with approximately 100% Faradaic yield.
format Online
Article
Text
id pubmed-8479727
institution National Center for Biotechnology Information
language English
publishDate 2021
publisher American Chemical Society
record_format MEDLINE/PubMed
spelling pubmed-84797272021-09-29 Bioelectrocatalytic Activity of W-Formate Dehydrogenase Covalently Immobilized on Functionalized Gold and Graphite Electrodes Alvarez-Malmagro, Julia Oliveira, Ana R. Gutiérrez-Sánchez, Cristina Villajos, Beatriz Pereira, Inês A.C. Vélez, Marisela Pita, Marcos De Lacey, Antonio L. ACS Appl Mater Interfaces [Image: see text] The decrease of greenhouse gases such as CO(2) has become a key challenge for the human kind and the study of the electrocatalytic properties of CO(2)-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 CO(2) 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 CO(2) electroreduction to formate by DET is shown with approximately 100% Faradaic yield. American Chemical Society 2021-03-03 2021-03-17 /pmc/articles/PMC8479727/ /pubmed/33656858 http://dx.doi.org/10.1021/acsami.0c21932 Text en © 2021 American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Alvarez-Malmagro, Julia
Oliveira, Ana R.
Gutiérrez-Sánchez, Cristina
Villajos, Beatriz
Pereira, Inês A.C.
Vélez, Marisela
Pita, Marcos
De Lacey, Antonio L.
Bioelectrocatalytic Activity of W-Formate Dehydrogenase Covalently Immobilized on Functionalized Gold and Graphite Electrodes
title Bioelectrocatalytic Activity of W-Formate Dehydrogenase Covalently Immobilized on Functionalized Gold and Graphite Electrodes
title_full Bioelectrocatalytic Activity of W-Formate Dehydrogenase Covalently Immobilized on Functionalized Gold and Graphite Electrodes
title_fullStr Bioelectrocatalytic Activity of W-Formate Dehydrogenase Covalently Immobilized on Functionalized Gold and Graphite Electrodes
title_full_unstemmed Bioelectrocatalytic Activity of W-Formate Dehydrogenase Covalently Immobilized on Functionalized Gold and Graphite Electrodes
title_short Bioelectrocatalytic Activity of W-Formate Dehydrogenase Covalently Immobilized on Functionalized Gold and Graphite Electrodes
title_sort bioelectrocatalytic activity of w-formate dehydrogenase covalently immobilized on functionalized gold and graphite electrodes
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8479727/
https://www.ncbi.nlm.nih.gov/pubmed/33656858
http://dx.doi.org/10.1021/acsami.0c21932
work_keys_str_mv AT alvarezmalmagrojulia bioelectrocatalyticactivityofwformatedehydrogenasecovalentlyimmobilizedonfunctionalizedgoldandgraphiteelectrodes
AT oliveiraanar bioelectrocatalyticactivityofwformatedehydrogenasecovalentlyimmobilizedonfunctionalizedgoldandgraphiteelectrodes
AT gutierrezsanchezcristina bioelectrocatalyticactivityofwformatedehydrogenasecovalentlyimmobilizedonfunctionalizedgoldandgraphiteelectrodes
AT villajosbeatriz bioelectrocatalyticactivityofwformatedehydrogenasecovalentlyimmobilizedonfunctionalizedgoldandgraphiteelectrodes
AT pereirainesac bioelectrocatalyticactivityofwformatedehydrogenasecovalentlyimmobilizedonfunctionalizedgoldandgraphiteelectrodes
AT velezmarisela bioelectrocatalyticactivityofwformatedehydrogenasecovalentlyimmobilizedonfunctionalizedgoldandgraphiteelectrodes
AT pitamarcos bioelectrocatalyticactivityofwformatedehydrogenasecovalentlyimmobilizedonfunctionalizedgoldandgraphiteelectrodes
AT delaceyantoniol bioelectrocatalyticactivityofwformatedehydrogenasecovalentlyimmobilizedonfunctionalizedgoldandgraphiteelectrodes