Identification of a key catalytic intermediate demonstrates that nitrogenase is activated by the reversible exchange of N₂ for H₂. - Wikidata - awgldk - TriplyDB

Identification of a key catalytic intermediate demonstrates that nitrogenase is activated by the reversible exchange of N₂ for H₂.

Identification of a key catalytic intermediate demonstrates that nitrogenase is activated by the reversible exchange of N₂ for H₂.

http://www.wikidata.org/entity/Q42553068

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A Synthetic Single-Site Fe Nitrogenase: High Turnover, Freeze-Quench (57)Fe Mössbauer Data, and a Hydride Resting State Insight into the Iron-Molybdenum Cofactor of Nitrogenase from Synthetic Iron Complexes with Sulfur, Carbon, and Hydride Ligands Light-driven dinitrogen reduction catalyzed by a CdS:nitrogenase MoFe protein biohybrid.Synthesis, Characterization, and Nitrogenase-Relevant Reactions of an Iron Sulfide Complex with a Bridging Hydride.X-ray Absorption and Emission Spectroscopic Studies of [L2Fe2S2](n) Model Complexes: Implications for the Experimental Evaluation of Redox States in Iron-Sulfur Clusters.Stepwise N-H Bond Formation From N2-Derived Iron Nitride, Imide and Amide Intermediates to Ammonia.Reversible Protonated Resting State of the Nitrogenase Active Site.Reversible Photoinduced Reductive Elimination of H2 from the Nitrogenase Dihydride State, the E(4)(4H) Janus Intermediate.Nitrogenase Cofactor: Inspiration for Model Chemistry.Reductive Elimination of H2 Activates Nitrogenase to Reduce the N≡N Triple Bond: Characterization of the E4(4H) Janus Intermediate in Wild-Type Enzyme.The Mechanism of N-N Double Bond Cleavage by an Iron(II) Hydride Complex CO2 Reduction Catalyzed by Nitrogenase: Pathways to Formate, Carbon Monoxide, and Methane.Exploring Electron/Proton Transfer and Conformational Changes in the Nitrogenase MoFe Protein and FeMo-cofactor Through Cryoreduction/EPR Measurements.Photoinduced Reductive Elimination of H2 from the Nitrogenase Dihydride (Janus) State Involves a FeMo-cofactor-H2 Intermediate.Mechanism of Nitrogenase H2 Formation by Metal-Hydride Protonation Probed by Mediated Electrocatalysis and H/D Isotope Effects.Synthesis and Characterization of Bioinspired [Mo2 Fe2 ]-Hydride Cluster Complexes and Their Application in the Catalytic Silylation of N2.Co6 H8 (Pi Pr3 )6 : A Cobalt Octahedron with Face-Capping Hydrides.The Mechanism of N2 Reduction Catalyzed by Fe-Nitrogenase Involves Reductive Elimination of H2.Is there computational support for an unprotonated carbon in the E4 state of nitrogenase?Interplay of hemilability and redox activity in models of hydrogenase active sites.

P2860

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P2860

Identification of a key catalytic intermediate demonstrates that nitrogenase is activated by the reversible exchange of N₂ for H₂.

http://www.wikidata.org/entity/Q42553068

description

2015 nî lūn-bûn

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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2015年论文

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2015年论文

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name

Identification of a key cataly ...... ersible exchange of N₂ for H₂.

@en

Identification of a key cataly ...... ersible exchange of N₂ for H₂.

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type

label

Identification of a key cataly ...... ersible exchange of N₂ for H₂.

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Identification of a key cataly ...... ersible exchange of N₂ for H₂.

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prefLabel

Identification of a key cataly ...... ersible exchange of N₂ for H₂.

@en

Identification of a key cataly ...... ersible exchange of N₂ for H₂.

@nl

P1433

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P1433

Journal of the American Chemical Society

P1476

Identification of a key cataly ...... versible exchange of N₂ for H₂

@en

P2093

Brian M Hoffman

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

Dennis R Dean

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Dmitriy Lukoyanov

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

Nimesh Khadka

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P2860

Mechanism of nitrogen fixation by nitrogenase: the next stage

Nitrogenase: a draft mechanism

On reversible H2 loss upon N2 binding to FeMo-cofactor of nitrogenase.

Mechanism of Mo-dependent nitrogenase

Trapping an intermediate of dinitrogen (N2) reduction on nitrogenase

Duplication and extension of the Thorneley and Lowe kinetic model for Klebsiella pneumoniae nitrogenase catalysis using a MATHEMATICA software platform.

Mechanism of Molybdenum Nitrogenase.

57Fe ENDOR spectroscopy and 'electron inventory' analysis of the nitrogenase E4 intermediate suggest the metal-ion core of FeMo-cofactor cycles through only one redox couple

A nitrogen pressure of 50 atmospheres does not prevent evolution of hydrogen by nitrogenase.

Trapping H- bound to the nitrogenase FeMo-cofactor active site during H2 evolution: characterization by ENDOR spectroscopy.

P304

3610-3615

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scholarly article

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10.1021/JACS.5B00103

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10

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137

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Lance C Seefeldt

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2015-03-05T00:00:00Z

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25741750

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