Characterization of the oxygen-tolerant formate dehydrogenase from Clostridium carboxidivorans.

ABSTRACT: Fixation of CO₂ into the organic compound formate by formate dehydrogenases (FDHs) is regarded as the oldest autotrophic process on Earth. It has been proposed that an FDH-dependent CO₂ fixation module could support CO₂ assimilation even in photoautotrophic organisms. In the present study, we characterized FDH from Clostridium carboxidivorans (ccFDH) due to its ability to reduce CO₂ under aerobic conditions. During the production of recombinant ccFDH, in which the selenocysteine codon was replaced by Cys, we were able to replace the W with Mo as the transition metal in the ccFDH metal cofactor, resulting in a two-fold increase of 6 μmol formate min^-1 in enzyme activity. Then, we generated ccFDH varian

SUBMITTER: Brouwer EM 

PROVIDER: S-EPMC11770034 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature