NADP(H)-dependent biocatalysis without adding NADP(H).

ABSTRACT: Isocitrate dehydrogenase 1 (IDH1) naturally copurifies and crystallizes in a resting state with a molecule of its exchangeable cofactor, NADP⁺/NADPH, bound in each monomer of the homodimer. We report electrochemical studies with IDH1 that exploit this property to reveal the massive advantage of nanoconfinement to increase the efficiency of multistep enzyme-catalyzed cascade reactions. When coloaded with ferredoxin NADP⁺ reductase in a nanoporous conducting indium tin oxide film, IDH1 carries out the complete electrochemical oxidation of 6 mM isocitrate (in 4mL) to 2-oxoglutarate (2OG), using only the NADP(H) that copurified with IDH1 and was carried into the electrode pores as cargo-the system remains active for days. The entrapped cofactor, now quantifiable by cyclic

SUBMITTER: Herold RA 

PROVIDER: S-EPMC9910440 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature