Electrocatalysis of CO 2 Reduction by Immobilized Formate Dehydrogenase without a Metal Redox Center.

Autor: Su Z; Electrochemical Technology Center, Department of Chemistry, University of Guelph, Guelph, Ontario N1G 2W1, Canada., Elmahdy R; Electrochemical Technology Center, Department of Chemistry, University of Guelph, Guelph, Ontario N1G 2W1, Canada., Biernat JF; Department of Chemistry, Gdansk University of Technology, Gdańsk 80-233, Poland., Chen A; Electrochemical Technology Center, Department of Chemistry, University of Guelph, Guelph, Ontario N1G 2W1, Canada., Lipkowski J; Electrochemical Technology Center, Department of Chemistry, University of Guelph, Guelph, Ontario N1G 2W1, Canada.
Jazyk: angličtina
Zdroj: Langmuir : the ACS journal of surfaces and colloids [Langmuir] 2024 Aug 06; Vol. 40 (31), pp. 16249-16257. Date of Electronic Publication: 2024 Jul 27.
DOI: 10.1021/acs.langmuir.4c01444
Abstrakt: Nicotinamide adenine dinucleotide-dependent formate dehydrogenase from Candida boidinii was immobilized in a 1,2-dimyristoyl- sn -glycero-3-phosphocholine/cholesterol floating lipid bilayer on the gold surface as a biocatalyst for electrochemical CO 2 reduction. We report that, in contrast to common belief, the enzyme can catalyze the electrochemical reduction of CO 2 to formate without the cofactor protonated nicotinamide adenine dinucleotide. The electrochemical data indicate that the enzyme-catalyzed reduction of CO 2 is diffusion-controlled and is a reversible reaction. The orientation and conformation of the enzyme were investigated by surface-enhanced infrared reflection absorption spectroscopy. The α-helix of the enzyme adopts an orientation nearly parallel to the surface, bringing its active center close to the gold surface. This orientation allows direct electron transfer between CO 2 and the gold electrode. The results in this paper provide a new method for the development of enzymatic electrocatalysts for CO 2 reduction.
Databáze: MEDLINE
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