A Genetically Encoded Redox-Active Nicotinamide Amino Acid.

ABSTRACT: Nicotinamide-containing cofactors play an essential role in many enzymes that catalyze two-electron redox reactions. However, it is difficult to engineer nicotinamide binding sites into proteins due to the extended nature of the cofactor-protein interface and the precise orientation of the nicotinamide moiety required for efficient electron transfer to or from the substrate. To address these challenges, we genetically encoded a noncanonical amino acid (ncAA) bearing a nicotinamide side chain in bacteria. This redox-active amino acid, termed Nic1, exhibits similar electrochemical properties to the natural cofactor nicotinamide adenine dinucleotide (NAD⁺). Nic1 can be reversibly reduced and oxidized using chemical reagents both free in solution and when incorporated into a model p

SUBMITTER: Pigula ML 

PROVIDER: S-EPMC11797079 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature