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Literature DB >> 19009086

A proton-hydride diiron complex with a base-containing diphosphine ligand relevant to the [FeFe]-hydrogenase active site.

Ning Wang¹, Mei Wang, Tingting Zhang, Ping Li, Jihong Liu, Licheng Sun.

Abstract

A diiron dithiolate complex holding a mu-hydride on the iron atoms and a proton on the basic site of a chelating diphosphine ligand was prepared and crystallographically characterized as a structural model of the [FeFe]-hydrogenase active site, and its molecular structure shows the H(mu)(-)...H(N)(+) distance is 3.934 A.

Entities: Chemical Disease

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Year: 2008 PMID： 19009086 DOI： 10.1039/b811352a

Source DB: PubMed Journal: Chem Commun (Camb) ISSN： 1359-7345 Impact factor: 6.222

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Cited

8 in total

Review 1. Hydrogenase Enzymes and Their Synthetic Models: The Role of Metal Hydrides.

Authors: David Schilter; James M Camara; Mioy T Huynh; Sharon Hammes-Schiffer; Thomas B Rauchfuss
Journal: Chem Rev Date: 2016-06-29 Impact factor: 60.622

2. Mechanisms for the synthesis of conjugated enynes from diphenylacetylene and trimethylsilylacetylene catalyzed by a nickel(0) complex: DFT study of ligand-controlled selectivity.

Authors: Cheng Huang; Rongxing He; Wei Shen; Ming Li
Journal: J Mol Model Date: 2015-05-03 Impact factor: 1.810

3. Favorable Protonation of the (μ-edt)[Fe(2)(PMe(3))(4)(CO)(2)(H-terminal)](+) Hydrogenase Model Complex Over Its Bridging μ-H Counterpart: A Spectroscopic and DFT Study.

Authors: Mary Grace I Galinato; C Matthew Whaley; Dean Roberts; Peng Wang; Nicolai Lehnert
Journal: Eur J Inorg Chem Date: 2011-03 Impact factor: 2.524

4. Vibrational analysis of the model complex (mu-edt)[Fe(CO)(3)](2) and comparison to iron-only hydrogenase: the activation scale of hydrogenase model systems.

Authors: Mary Grace I Galinato; C Matthew Whaley; Nicolai Lehnert
Journal: Inorg Chem Date: 2010-04-05 Impact factor: 5.165

5. Cobalt and nickel diimine-dioxime complexes as molecular electrocatalysts for hydrogen evolution with low overvoltages.

Authors: Pierre-André Jacques; Vincent Artero; Jacques Pécaut; Marc Fontecave
Journal: Proc Natl Acad Sci U S A Date: 2009-11-30 Impact factor: 11.205

A proton-hydride diiron complex with a base-containing diphosphine ligand relevant to the [FeFe]-hydrogenase active site.

Review 1. Hydrogenase Enzymes and Their Synthetic Models: The Role of Metal Hydrides.

2. Mechanisms for the synthesis of conjugated enynes from diphenylacetylene and trimethylsilylacetylene catalyzed by a nickel(0) complex: DFT study of ligand-controlled selectivity.

3. Favorable Protonation of the (μ-edt)[Fe(2)(PMe(3))(4)(CO)(2)(H-terminal)](+) Hydrogenase Model Complex Over Its Bridging μ-H Counterpart: A Spectroscopic and DFT Study.

4. Vibrational analysis of the model complex (mu-edt)[Fe(CO)(3)](2) and comparison to iron-only hydrogenase: the activation scale of hydrogenase model systems.

5. Cobalt and nickel diimine-dioxime complexes as molecular electrocatalysts for hydrogen evolution with low overvoltages.

6. Hydrogen activation by biomimetic [NiFe]-hydrogenase model containing protected cyanide cofactors.

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

8. Hydrogenase Mimics in M₁₂ L₂₄ Nanospheres to Control Overpotential and Activity in Proton-Reduction Catalysis.