Increasing the O₂ Resistance of the [FeFe]-Hydrogenase CbA5H through Enhanced Protein Flexibility.

ABSTRACT: The high turnover rates of [FeFe]-hydrogenases under mild conditions and at low overpotentials provide a natural blueprint for the design of hydrogen catalysts. However, the unique active site (H-cluster) degrades upon contact with oxygen. The [FeFe]-hydrogenase fromClostridium beijerinckii (CbA5H) is characterized by the flexibility of its protein structure, which allows a conserved cysteine to coordinate to the active site under oxidative conditions. Thereby, intrinsic cofactor degradation induced by dioxygen is minimized. However, the protection from O₂ is only partial, and the activity of the enzyme decreases upon each exposure to O₂. By using site-directed mutagenesis in combination with electrochemistry, ATR-FTIR spectroscopy, and molecular dynamics simul

SUBMITTER: Rutz A 

PROVIDER: S-EPMC9886219 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature