Mimicking the Electron Transport Chain and Active Site of [FeFe] Hydrogenases in One Metal-Organic Framework: Factors That Influence Charge Transport.

ABSTRACT: [FeFe] hydrogenase (H₂ase) enzymes are effective proton reduction catalysts capable of forming molecular dihydrogen with a high turnover frequency at low overpotential. The active sites of these enzymes are buried within the protein structures, and substrates required for hydrogen evolution (both protons and electrons) are shuttled to the active sites through channels from the protein surface. Metal-organic frameworks (MOFs) provide a unique platform for mimicking such enzymes due to their inherent porosity which permits substrate diffusion and their structural tunability which allows for the incorporation of multiple functional linkers. Herein, we describe the preparation and characterization of a redox-active PCN-700-based MOF (PCN = porous coordination network) that features

SUBMITTER: Castner AT 

PROVIDER: S-EPMC8176456 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature