Switching Site Reactivity in Hydrogenase Model Systems by Introducing a Pendant Amine Ligand.

ABSTRACT: Hydrogenases are versatile enzymatic catalysts with an unmet hydrogen evolution reactivity (HER) from synthetic bio-inspired systems. The binuclear active site only has one-site reactivity of the distal Fe_d atom. Here, binuclear complexes [Fe₂(CO)₅(μ-Mebdt)(P(4-C₆H₄OCH₃)₃)] 1 and [Fe₂(CO)₅(μ-Mebdt)(PPh₂Py)] 2 are presented, which show electrocatalytic activity in the presence of weak acids as a proton source for the HER. Despite almost identical structural and spectroscopic properties (bond distances and angles from single-crystal X-ray; IR, UV/vis, and NMR), introduction of a nitrogen base atom in the phosphine ligand in 2 markedly changes site reactivity. The

SUBMITTER: Pandey IK 

PROVIDER: S-EPMC7906588 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature