Open AccessBioelectrocatalytic Activity of W-Formate Dehydrogenase Covalently Immobilized on Functionalized Gold and Graphite Electrodes
Author(s) -
Julia Álvarez-Malmagro,
Ana Rita Oliveira,
Cristina Gutiérrez-Sánchez,
Beatriz Villajos,
Inês A. C. Pereira,
Marisela Vélez,
Marcos Pita,
Antonio L. De Lacey
Publication year - 2021
Publication title -
acs applied materials and interfaces
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.535
H-Index - 228
eISSN - 1944-8252
pISSN - 1944-8244
DOI - 10.1021/acsami.0c21932
Subject(s) - formate , formate dehydrogenase , materials science , electrocatalyst , electrochemistry , quartz crystal microbalance , electrode , covalent bond , faraday efficiency , chemical engineering , electron transfer , inorganic chemistry , graphite , nanotechnology , chemistry , organic chemistry , adsorption , catalysis , composite material , engineering
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.