ArticleInorganic chemistry2016
Models of the Ni-L and Ni-SIa States of the [NiFe]-Hydrogenase Active Site.
Article in Inorganic chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed.
- NRVS Spectroscopy Resolves Distinct Bridging Hydride Intermediates in [NiFe]-Hydrogenase.Journal of the American Chemical Society · 2025Article
- Magnetic interactions between metal sites in complex enzymes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Review
- How Geometric Constraints Control the Hydride Position and Activity in [NiFe]-Hydrogenases and Their Biomimetic Complexes.Inorganic chemistry · 2025Article
- The Fully Oxidized State of the Glutamate Coordinated OJournal of the American Chemical Society · 2023Article
- Characterization of paramagnetic states in an organometallic nickel hydrogen evolution electrocatalyst.Nature communications · 2023Article
- Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase.Chemical reviews · 2022Review
- Heterodinuclear nickel(ii)-iron(ii) azadithiolates as structural and functional models for the active site of [NiFe]-hydrogenases.RSC advances · 2020Article
- The large subunit of the regulatory [NiFe]-hydrogenase fromChemical science · 2020Article
- Bimetallic nickel-cobalt hydrides in HChemical science · 2019Article
- Synthetic Models for Nickel-Iron Hydrogenase Featuring Redox-Active Ligands.Australian journal of chemistry · 2017Article
- Nickel-centred proton reduction catalysis in a model of [NiFe] hydrogenase.Nature chemistry · 2016Article
- Hydrogenase Enzymes and Their Synthetic Models: The Role of Metal Hydrides.Chemical reviews · 2016Review
- Mechanism of H2 Production by Models for the [NiFe]-Hydrogenases: Role of Reduced Hydrides.Journal of the American Chemical Society · 2016Article
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Abstract
A new class of synthetic models for the active site of [NiFe]-hydrogenases are described. The Ni(I/II)(SCys)2 and Fe(II)(CN)2CO sites are represented with (RC5H4)Ni(I/II) and Fe(II)(diphos)(CO) modules, where diphos = 1,2-C2H4(PPh2)2(dppe) or cis-1,2-C2H2(PPh2)2(dppv). The two bridging thiolate ligands are represented by CH2(CH2S)2(2-) (pdt(2-)), Me2C(CH2S)2(2-) (Me2pdt(2-)), and (C6H5S)2(2-). The reaction of Fe(pdt)(CO)2(dppe) and [(C5H5)3Ni2]BF4 affords [(C5H5)Ni(pdt)Fe(dppe)(CO)]BF4 ([1a]BF4). Monocarbonyl [1a]BF4 features an S = 0 Ni(II)Fe(II) center with five-coordinated iron, as proposed for the Ni-SIa state of the enzyme. One-electron reduction of [1a](+) affords the S = 1/2 derivative [1a](0), which, according to density functional theory (DFT) calculations and electron paramagnetic resonance and Mössbauer spectroscopies, is best described as a Ni(I)Fe(II) compound. The Ni(I)Fe(II) assignment matches that for the Ni-L state in [NiFe]-hydrogenase, unlike recently reported Ni(II)Fe(I)-based models. Compound [1a](0) reacts with strong acids to liberate 0.5 equiv of H2 and regenerate [1a](+), indicating that H2 evolution is catalyzed by [1a](0). DFT calculations were used to investigate the pathway for H2 evolution and revealed that the mechanism can proceed through two isomers of [1a](0) that differ in the stereochemistry of the Fe(dppe)CO center. Calculations suggest that protonation of [1a](0) (both isomers) affords Ni(III)-H-Fe(II) intermediates, which represent mimics of the Ni-C state of the enzyme.
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