Dataset Information

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(?-Mebdt)(P(4-C₆H₄OCH₃)₃)] 1 and [Fe₂(CO)₅(?-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.

SUBMITTER: Pandey IK

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

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

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

Pandey Indresh Kumar IK Agarwal Tashika T Mobin Shaikh M SM Stein Matthias M Kaur-Ghumaan Sandeep S

ACS omega 20210202 6

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 Fed 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 presen ...[more]

PMID: 33644543

Similar Datasets

Project description:Research on simple [FeFe] hydrogenase model systems of type (mu-S(2)R)[Fe(CO)(3)](2) (R = C(2)H(4) (edt), C(3)H(6) (pdt)) which have been shown to function as robust electrocatalysts for proton reduction, provides a reference to understand the electronic and vibrational properties of the active site of [FeFe] hydrogenases and of more sophisticated model systems. In this study, the solution and solid state Raman spectra of (mu-edt)[Fe(CO)(3)](2) and of the corresponding (13)CO-labeled complex are presented and analyzed in detail, with focus on the nu(C=O) and nu(Fe-CO)/delta(Fe-C=O) vibrational regions. These regions are specifically important as vibrations involving CO ligands serve as probes for the "electron richness" of low-valent transition metal centers and the geometric structures of the complexes. The obtained vibrational spectra have been completely assigned in terms of the nu(C=O), nu(Fe-CO), and delta(Fe-C=O) modes, and the force constants of the important C=O and Fe-CO bonds have been determined using our Quantum Chemistry Centered Normal Coordinate Analysis (QCC-NCA). In the 400-650 cm(-1) region, fifteen mixed nu(Fe-CO)/delta(Fe-C=O) modes have been identified. The most prominent Raman peaks at 454, 456, and 483 cm(-1) correspond to a combination of nu(Fe-CO) stretching and delta(Fe-C=O) linear bending modes. The less intense peaks at 416 cm(-1) and 419 cm(-1) correspond to pure delta(Fe-C=O) linear bends. In the nu(C=O) region, the nu(C=O) normal modes at lower energy (1968 and 1964 cm(-1)) are almost pure equatorial (eq) nu(C=O)(eq) stretching vibrations, whereas the remaining four nu(C=O) normal modes show dominant (C=O)(eq) (2070 and 1961 cm(-1)) and (C=O)(ax) (2005 and 1979 cm(-1); ax = axial) contributions. Importantly, an inverse correlation between the f(C=O)(ax/eq) and f(Fe-CO)(ax/eq) force constants is obtained, in agreement with the idea that the Fe(I)-CO bond in these types of complexes is dominated by pi-backdonation. Compared to the reduced form of [FeFe] hydrogenase (H(red)), the nu(C=O) vibrational frequencies of (mu-edt)[Fe(CO)(3)](2) are higher in energy, indicating that the dinuclear iron core in (mu-edt)[Fe(CO)(3)](2) is less electron rich compared to H(red) in the actual enzyme. Finally, quantum yields for the photodecomposition of (mu-edt)[Fe(CO)(3)](2) have been determined.

Dataset Information

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

Publications

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

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets