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

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 bridging benzenedithiolate ligand Mebdt interacts with the terminal ligand's phenyl aromatic rings and stabilizes the reduced states of the catalysts. Although 1 with monodentate phosphine terminal ligands only shows a distal iron atom HER activity by a sequence of electrochemical and protonation steps, the lone pair of pyridine nitrogen in 2 acts as the primary site of protonation. This swaps the iron atom catalytic activity toward the proximal iron for complex 2. Density-functional theory (DFT) calculations reveal the role of terminal phosphines ligands without/with pendant amines by directing the proton transfer steps. The reactivity of 1 is a thiol-based protonation of a dangling bond in 1 and distal iron hydride mechanism, which may follow either an ECEC or EECC sequence, depending on the choice of acid. The pendant amine in 2 enables a terminal ligand protonation and an ECEC reactivity. The introduction of a terminal nitrogen atom enables the control of site reactivity in a binuclear system.