Synthetic models for the active site of the [FeFe]-hydrogenase: catalytic proton reduction and the structure of the doubly protonated intermediate.
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X-ray Crystallographic, Multifrequency Electron Paramagnetic Resonance, and Density Functional Theory Characterization of the Ni(P(Cy)2N(tBu)2)2(n+) Hydrogen Oxidation Catalyst in the Ni(I) Oxidation StateFrontiers, opportunities, and challenges in biochemical and chemical catalysis of CO2 fixationSingly versus Doubly Reduced Nickel Porphyrins for Proton Reduction: Experimental and Theoretical Evidence for a Homolytic Hydrogen-Evolution ReactionTerminal vs bridging hydrides of diiron dithiolates: protonation of Fe2(dithiolate)(CO)2(PMe3)4.Computational investigation of [FeFe]-hydrogenase models: characterization of singly and doubly protonated intermediates and mechanistic insights.Hydrogen Production Catalyzed by Bidirectional, Biomimetic Models of the [FeFe]-Hydrogenase Active Site.Borane-protected cyanides as surrogates of H-bonded cyanides in [FeFe]-hydrogenase active site models.N-Substituted Derivatives of the Azadithiolate Cofactor from the [FeFe] Hydrogenases: Stability and ComplexationDiiron azadithiolates as models for the [FeFe]-hydrogenase active site and paradigm for the role of the second coordination sphereModels of the Ni-L and Ni-SIa States of the [NiFe]-Hydrogenase Active SitePreparation and Protonation of Fe2(pdt)(CNR)6, Electron-Rich Analogues of Fe2(pdt)(CO)6Synthesis of Diiron(I) Dithiolato Carbonyl ComplexesMechanism of H2 Production by Models for the [NiFe]-Hydrogenases: Role of Reduced Hydrides.Ferrous Carbonyl Dithiolates as Precursors to FeFe, FeCo, and FeMn Carbonyl Dithiolates.Hydrogenase Enzymes and Their Synthetic Models: The Role of Metal Hydrides.Frustration across the periodic table: heterolytic cleavage of dihydrogen by metal complexes.Nickel-centred proton reduction catalysis in a model of [NiFe] hydrogenase.Accumulating the hydride state in the catalytic cycle of [FeFe]-hydrogenases.And the winner is...azadithiolate: an amine proton relay in the [FeFe] hydrogenases.Hydrogen activation by biomimetic [NiFe]-hydrogenase model containing protected cyanide cofactors.Biomimetic assembly of the [FeFe] hydrogenase: synthetic mimics in a biological shell.Crystallographic characterization of a fully rotated, basic diiron dithiolate: model for the H(red) state?Heterolytic cleavage of hydrogen by an iron hydrogenase model: an Fe-H⋅⋅⋅H-N dihydrogen bond characterized by neutron diffraction.Direct Observation of an Iron-Bound Terminal Hydride in [FeFe]-Hydrogenase by Nuclear Resonance Vibrational Spectroscopy.Reaction Coordinate Leading to H2 Production in [FeFe]-Hydrogenase Identified by Nuclear Resonance Vibrational Spectroscopy and Density Functional Theory.Copper complexes as catalyst precursors in the electrochemical hydrogen evolution reaction.A reversible proton relay process mediated by hydrogen-bonding interactions in [FeFe]hydrogenase modeling.Redox communication within multinuclear iron-sulfur complexes related to electronic interplay in the active site of [FeFe]hydrogenase.New tetracobalt cluster compounds for electrocatalytic proton reduction: syntheses, structures, and reactivity.Increasing the rate of hydrogen oxidation without increasing the overpotential: a bio-inspired iron molecular electrocatalyst with an outer coordination sphere proton relay.DHPA-Containing Cobalt-Based Redox Metal-Organic Cyclohelicates as Enzymatic Molecular Flasks for Light-Driven H2 Production.Synthetic [NiFe] models with a fluxional CO ligand.A Functional Hydrogenase Mimic Chemisorbed onto Fluorine-Doped Tin Oxide Electrodes: A Strategy towards Water Splitting Devices.Interplay between Terminal and Bridging Diiron Hydrides in Neutral and Oxidized States.Graphene-Supported Pyrene-Modified Cobalt Corrole with Axial Triphenylphosphine for Enhanced Hydrogen Evolution in pH 0-14 Aqueous Solutions.Reactions of [FeFe]-hydrogenase models involving the formation of hydrides related to proton reduction and hydrogen oxidation.Sterically Stabilized Terminal Hydride of a Diiron Dithiolate.Selenium makes the difference: protonation of [FeFe]-hydrogenase mimics with diselenolato ligands.Catalytic Activity of Thiolate-Bridged Diruthenium Complexes Bearing Pendent Ether Moieties in the Oxidation of Molecular Dihydrogen.Diiron Dithiolate Hydrides Complemented with Proton-Responsive Phosphine-Amine Ligands.
P2860
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P2860
Synthetic models for the active site of the [FeFe]-hydrogenase: catalytic proton reduction and the structure of the doubly protonated intermediate.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh
2012年學術文章
@zh-hant
name
Synthetic models for the activ ...... oubly protonated intermediate.
@ast
Synthetic models for the activ ...... oubly protonated intermediate.
@en
type
label
Synthetic models for the activ ...... oubly protonated intermediate.
@ast
Synthetic models for the activ ...... oubly protonated intermediate.
@en
prefLabel
Synthetic models for the activ ...... oubly protonated intermediate.
@ast
Synthetic models for the activ ...... oubly protonated intermediate.
@en
P2093
P2860
P356
P1476
Synthetic models for the activ ...... oubly protonated intermediate.
@en
P2093
Bryan E Barton
Maria E Carroll
Patrick J Carroll
Thomas B Rauchfuss
P2860
P304
18843-18852
P356
10.1021/JA309216V
P407
P577
2012-11-05T00:00:00Z