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Nickel-centred proton reduction catalysis in a model of NiFe hydrogenase
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Nickel-centred proton reduction catalysis in a model of NiFe hydrogenase
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Journal Article
Nickel-centred proton reduction catalysis in a model of NiFe hydrogenase
2016
Overview
Hydrogen production through water splitting is one of the most promising solutions for the storage of renewable energy. [NiFe] hydrogenases are organometallic enzymes containing nickel and iron centres that catalyse hydrogen evolution with performances that rival those of platinum. These enzymes provide inspiration for the design of new molecular catalysts that do not require precious metals. However, all heterodinuclear NiFe models reported so far do not reproduce the Ni-centred reactivity found at the active site of [NiFe] hydrogenases. Here, we report a structural and functional NiFe mimic that displays reactivity at the Ni site. This is shown by the detection of two catalytic intermediates that reproduce structural and electronic features of the Ni-L and Ni-R states of the enzyme during catalytic turnover. Under electrocatalytic conditions, this mimic displays high rates for H
2
evolution (second-order rate constant of 2.5 × 10
4
M
−1
s
−1
; turnover frequency of 250 s
−1
at 10 mM H
+
concentration) from mildly acidic solutions.
[NiFe] hydrogenases are enzymes containing nickel and iron centres that catalyse hydrogen evolution with performances that rival those of platinum catalysts. Now, a NiFe model complex has been reported that mimics the structure and the Ni-centred hydrogen evolution activity found at the active site of [NiFe] hydrogenases.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 140/131
/ 140/58
/ Biomimetic Materials - chemical synthesis
/ Biomimetic Materials - chemistry
/ Biomimetic Materials - metabolism
/ Coordination Complexes - chemical synthesis
/ Coordination Complexes - chemistry
/ Electron Spin Resonance Spectroscopy
/ Enzymes
/ Hydrogen
/ Ligands
/ Nickel
/ Protons
