Chemists have long sought to mimic enzymatic hydrogen activation with structurally simpler compounds. Here, we report a functional [NiFe]-based model of [NiFe]hydrogenase enzymes. This complex heterolytically activates hydrogen to form a hydride complex that is capable of reducing substrates by either hydride ion or electron transfer. Structural investigations were performed by a range of techniques, including x-ray diffraction and neutron scattering, resulting in crystal structures and the finding that the hydrido ligand is predominantly associated with the Fe center. The ligand's hydridic character is manifested in its reactivity with strong acid to liberate H(2).
Dioxygen-tolerant [NiFe] hydrogenases catalyze not only the conversion of H2 into 2 H(+) and 2 e(-) but also the reduction of O2 to H2O. Chemists have sought to mimic such bifunctional catalysts with structurally simpler compounds to facilitate analysis and improvement. Herein, we report a new [NiFe]-based catalyst for O2 reduction via an O2 adduct. Structural investigations reveal the first example of a side-on iron(IV) peroxo complex.
The study of hydrogenase enzymes (H2ases) is necessary because of their importance to a future hydrogen energy economy. These enzymes come in three distinct classes: [NiFe] H2ases, which have a propensity toward H2 oxidation; [FeFe] H2ases, which have a propensity toward H2 evolution; and [Fe] H2ases, which catalyze H− transfer. Modeling these enzymes has so far treated them as different species, which is understandable given the different cores and ligand sets of the natural molecules. Here, we demonstrate, using x-ray analysis and nuclear magnetic resonance, infrared, Mössbauer spectroscopies, and electrochemical measurement, that the catalytic properties of all three enzymes can be mimicked with only three isomers of the same NiFe complex.
We present two closely related series of a [NiFe] hydrogenase
analogue.
Based on a [NiRu] core, these complexes demonstrate inactivity, H2 activation, or O2 activation depending only on
the nature of the Ru-coordinated aromatic ligand. It is demonstrated
that even small changes made to this aromatic ligand can modulate
the catalytic activity of the complex. Structural, electrochemical,
kinetic, and thermodynamic studies reveal that differences in activation
and binding modes of the substrates, combined with differences in
σ donation and lability of the aromatic ligands, result in abrupt
changes in catalytic activity.
We present a mechanistic investigation for the activation of H 2 and O 2 , induced by a simple ligand effect within [NiFe] models for O 2 -tolerant [NiFe]hydrogenase. Kinetic study reveals Michaelis−Menten type saturation behaviors for both H 2 and O 2 activation, which is the same behavior as that found in O 2 -tolerant [NiFe]hydrogenase. Such saturation behavior is caused by H 2 complexation followed by heterolytic cleavage of H 2 by an outer-sphere base, resulting in the formation of a hydride species showing hydridic character.
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