A functional [NiFe]hydrogenase mimic that catalyzes electron and hydride transfer from H2. - Wikidata - awgldk - TriplyDB

A functional [NiFe]hydrogenase mimic that catalyzes electron and hydride transfer from H2.

A functional [NiFe]hydrogenase mimic that catalyzes electron and hydride transfer from H2.

http://www.wikidata.org/entity/Q44765295

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Hydride bridge in [NiFe]-hydrogenase observed by nuclear resonance vibrational spectroscopy Hydrogens detected by subatomic resolution protein crystallography in a [NiFe] hydrogenase Mechanism of hydrogen activation by [NiFe] hydrogenases Synthetic Active Site Model of the [NiFeSe] Hydrogenase Chinese puzzle molecule: a 15 hydride, 28 copper atom nanoball.Advanced paramagnetic resonance spectroscopies of iron-sulfur proteins: Electron nuclear double resonance (ENDOR) and electron spin echo envelope modulation (ESEEM)Catalytic hydrogen oxidation: dawn of a new iron age.Models of the Ni-L and Ni-SIa States of the [NiFe]-Hydrogenase Active Site Mechanism of H2 Production by Models for the [NiFe]-Hydrogenases: Role of Reduced Hydrides.De novo design of functional proteins: Toward artificial hydrogenases.Synthesis and characterization of a family of thioether-dithiolate-bridged heteronuclear iron complexes.Proton Transfer in the Catalytic Cycle of [NiFe] Hydrogenases: Insight from Vibrational Spectroscopy.Hydrogenase Enzymes and Their Synthetic Models: The Role of Metal Hydrides.Towards [NiFe]-hydrogenase biomimetic models that couple H2 binding with functionally relevant intramolecular electron transfers: a quantum chemical study.Frustration across the periodic table: heterolytic cleavage of dihydrogen by metal complexes.In search of metal hydrides: an X-ray absorption and emission study of [NiFe] hydrogenase model complexes.Nickel-centred proton reduction catalysis in a model of [NiFe] hydrogenase.Hydrogen activation by biomimetic [NiFe]-hydrogenase model containing protected cyanide cofactors.Catalytic hydrogen production by a Ni-Ru mimic of NiFe hydrogenases involves a proton-coupled electron transfer step.Heterolytic cleavage of hydrogen by an iron hydrogenase model: an Fe-H⋅⋅⋅H-N dihydrogen bond characterized by neutron diffraction.Light-Driven Hydrogen Evolution by Nickel-Substituted Rubredoxin.Synthetic Models for Nickel-Iron Hydrogenase Featuring Redox-Active Ligands.An Unsaturated Four-Coordinate Dimethyl Dimolybdenum Complex with a Molybdenum-Molybdenum Quadruple Bond.A Ni(i)Fe(ii) analogue of the Ni-L state of the active site of the [NiFe] hydrogenases.Synthesis, characterization and reactivity studies of electrophilic ruthenium(II) complexes: a study of H₂ activation and labilization.Increasing the rate of hydrogen oxidation without increasing the overpotential: a bio-inspired iron molecular electrocatalyst with an outer coordination sphere proton relay.Synthetic [NiFe] models with a fluxional CO ligand.From Enzymes to Functional Materials-Towards Activation of Small Molecules.Reconstitution of [Fe]-hydrogenase using model complexes.Dithiolato-bridged nickel-iron complexes as models for the active site of [NiFe]-hydrogenases.Catalytic Activity of Thiolate-Bridged Diruthenium Complexes Bearing Pendent Ether Moieties in the Oxidation of Molecular Dihydrogen.A redox hydrogel protects hydrogenase from high-potential deactivation and oxygen damage.Supramolecular self-assembly of heterobimetallic complexes: a new N,P-based, selective heteroditopic ligand.One Model, Two Enzymes: Activation of Hydrogen and Carbon Monoxide.An S-Oxygenated [NiFe] Complex Modelling Sulfenate Intermediates of an O2 -Tolerant Hydrogenase.A High-Valent Iron(IV) Peroxo Core Derived from O2.Nitrogen heterocyclic carbene containing pentacoordinate iron dicarbonyl as a [Fe]-hydrogenase active site model.Interplay of hemilability and redox activity in models of hydrogenase active sites.Dithiolato- and halogenido-bridged nickel-iron complexes related to the active site of [NiFe]-H2ases: preparation, structures, and electrocatalytic H2 production.A matrix of heterobimetallic complexes for interrogation of hydrogen evolution reaction electrocatalysts.

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P2860

A functional [NiFe]hydrogenase mimic that catalyzes electron and hydride transfer from H2.

http://www.wikidata.org/entity/Q44765295

description

2013 nî lūn-bûn

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2013年の論文

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2013年学术文章

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2013年学术文章

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2013年学术文章

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2013年学术文章

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2013年学术文章

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2013年学术文章

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2013年學術文章

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2013年學術文章

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name

A functional [NiFe]hydrogenase ...... and hydride transfer from H2.

@en

A functional [NiFe]hydrogenase ...... and hydride transfer from H2.

@nl

type

label

A functional [NiFe]hydrogenase ...... and hydride transfer from H2.

@en

A functional [NiFe]hydrogenase ...... and hydride transfer from H2.

@nl

prefLabel

A functional [NiFe]hydrogenase ...... and hydride transfer from H2.

@en

A functional [NiFe]hydrogenase ...... and hydride transfer from H2.

@nl

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SCIENCE.1231345

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P1476

A functional [NiFe]hydrogenase ...... and hydride transfer from H2.

@en

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Katsuhiro Kusaka

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Koji Ichikawa

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Seiji Ogo

http://www.w3.org/2001/XMLSchema#string

Takahiro Kishima

http://www.w3.org/2001/XMLSchema#string

Takahiro Matsumoto

http://www.w3.org/2001/XMLSchema#string

P2860

Removal of the bridging ligand atom at the Ni-Fe active site of [NiFe] hydrogenase upon reduction with H2, as revealed by X-ray structure analysis at 1.4 A resolution

The finer things in X-ray diffraction data collection

Structural and functional analogues of the active sites of the [Fe]-, [NiFe]-, and [FeFe]-hydrogenases

A dinuclear Ni(mu-H)Ru complex derived from H2.

Small molecule mimics of hydrogenases: hydrides and redox.

Better than platinum? Fuel cells energized by enzymes.

Fundamentals of H2 binding and reactivity on transition metals underlying hydrogenase function and H2 production and storage.

Electrons from hydrogen.

Nickel-iron dithiolato hydrides relevant to the [NiFe]-hydrogenase active site.

Intramolecular kinetic isotope effect in hydride transfer from dihydroacridine to a quinolinium ion. Rejection of a proposed two-step mechanism with a kinetically significant intermediate.

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682-684

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scholarly article

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10.1126/SCIENCE.1231345

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339

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