In vitro sulfuration of Rhodobacter capsulatus formate dehydrogenase.

ABSTRACT: Metal-dependent formate dehydrogenases (FDHs) are of considerable interest as a bioinspired metalloenzyme target to efficiently reduce the greenhouse gas CO₂ into the portable energy carrier formate under physiological conditions. These enzymes were shown to harbor an active site sulfido ligand that is essential for the formate oxidation and CO₂ reduction activity and contributes to the oxygen sensitivity of the enzyme, since the ligand is rapidly lost in the presence of O₂. Inhibitors like azide or nitrate are routinely employed to protect the active site from oxidative damage. The demonstrated unitary in vitro sulfido ligand incorporation to the active site bis metal-binding pterin guanine dinucleotide (bis-MGD) cofactor in FDH from Rhodobacter capsulatus

SUBMITTER: Duffus BR 

PROVIDER: S-EPMC12140954 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature