Formate Dehydrogenases Reduce CO2 Rather than HCO3−: An Electrochemical Demonstration. (18th March 2021)

• Record Type: Journal Article
• Authors: Meneghello, Marta; Oliveira, Ana Rita; Jacq‐Bailly, Aurore; Pereira, Inês A. C.; Léger, Christophe; Fourmond, Vincent
• Is Part Of: Angewandte Chemie. Volume 133:Number 18(2021)
• Page Start: 10052
• Page End: 10055
• Publication Date: 2021-03-18
• Subjects: bioelectrochemistry -- carbonic anhydrase -- CO dehydrogenase -- CO2 reduction -- protein film voltammetry; Chemistry -- Periodicals; 540
• DOI: 10.1002/ange.202101167
• Languages: English
• ISSNs: 0044-8249

Abstract

Abstract: Mo/W formate dehydrogenases catalyze the reversible reduction of CO2 species to formate. It is thought that the substrate is CO2 and not a hydrated species like HCO3 −, but there is still no indisputable evidence for this, in spite of the extreme importance of the nature of the substrate for mechanistic studies. We devised a simple electrochemical method to definitively demonstrate that the substrate of formate dehydrogenases is indeed CO2 . Abstract : A simple, inexpensive and fast method base on protein film electrochemistry is proposed to discriminate whether CO2 or HCO3 − is the substrate of any catalyst interacting with an electrode. In this study, CO2 rather than HCO3 − is found to be the substrate of both formate dehydrogenase and CO dehydrogenase.