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Hydrogenase Models
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DOI：10.1002/9781119951438.eibc2245.png)
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Abstract
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Abstract
This review will highlight major advances in the synthesis and study of active site analogs for the [NiFe]‐, [FeFe]‐, and [Fe]‐hydrogenases (H
2
ases). In their biological role, the [NiFe]‐ and [FeFe]‐
H
2
ases utilize a combination of redox and acid–base reactions for the activation and formation of H
2
. Both reactions have been demonstrated in models. Relevant to the [NiFe]‐H
2
ases, models have been developed that form hydrides via the biologically relevant pathways of protonation or activation of H
2
. These hydrides serve as catalysts for the reduction of protons or oxidation of H
2
via mixed‐valence intermediates. These studies suggest that the hydride bridges the two metals unsymmetrically, and the Fe–
H
…
Ni center engages in dihydrogen bonding to protic reagents as an intermediate in the formation and activation of H
2
. For the [FeFe]‐H
2
ases, the most informative models feature both an azadithiolate cofactor, which serves as a proton relay, and a terminal hydride ligand. Diiron species undergo oxidation to mixed‐valence Fe(I)Fe(
II
) cations, several of which are capable of oxidizing H
2
. The Fe(I)Fe(I) species catalyze hydrogen evolution via the formation of iron hydrides. Catalysis is faster when the hydride is a terminal ligand, but also proceeds for isomeric species with a bridging hydride ligand. Models for [Fe]‐H
2
ases feature biomimetic coordination spheres consisting of acyl, thiolate, and 2‐substituted pyridine ligands bound to a redox‐inactive ferrous center.
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