Spectroscopic and biochemical insight into an electron-bifurcating [FeFe] hydrogenase.

ABSTRACT: The heterotrimeric electron-bifurcating [FeFe] hydrogenase (HydABC) from Thermotoga maritima (Tm) couples the endergonic reduction of protons (H⁺) by dihydronicotinamide adenine dinucleotide (NADH) (∆G⁰ ≈ 18 kJ mol^-1) to the exergonic reduction of H⁺ by reduced ferredoxin (Fd_red) (∆G⁰ ≈ - 16 kJ mol^-1). The specific mechanism by which HydABC functions is not understood. In the current study, we describe the biochemical and spectroscopic characterization of TmHydABC recombinantly produced in Escherichia coli and artificially maturated with a synthetic diiron cofactor. We found that TmHydABC catalyzed the hydrogen (H₂)-dependent reduction of nicotinamide adenine dinucleotide (NAD⁺) in the presen

SUBMITTER: Chongdar N 

PROVIDER: S-EPMC7064455 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature