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

ABSTRACT: 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 electrocatalys

SUBMITTER: Alvarez-Malmagro J 

PROVIDER: S-EPMC8479727 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature