Changing the Electron Acceptor Specificity of Rhodobacter capsulatus Formate Dehydrogenase from NAD⁺ to NADP.

ABSTRACT: Formate dehydrogenases catalyze the reversible oxidation of formate to carbon dioxide. These enzymes play an important role in CO₂ reduction and serve as nicotinamide cofactor recycling enzymes. More recently, the CO₂-reducing activity of formate dehydrogenases, especially metal-containing formate dehydrogenases, has been further explored for efficient atmospheric CO₂ capture. Here, we investigate the nicotinamide binding site of formate dehydrogenase from Rhodobacter capsulatus for its specificity toward NAD⁺ vs. NADP⁺ reduction. Starting from the NAD⁺-specific wild-type RcFDH, key residues were exchanged to enable NADP⁺ binding on the basis of the NAD⁺-bound cryo-EM structure (PDB-ID: 6T

SUBMITTER: Kumar H 

PROVIDER: S-EPMC10671435 | biostudies-literature | 2023 Nov

REPOSITORIES: biostudies-literature