Combining acid-base, redox and substrate binding functionalities to give a complete model for the [FeFe]-hydrogenase.
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Proteins as templates for complex synthetic metalloclusters: towards biologically programmed heterogeneous catalysisAn iron-iron hydrogenase mimic with appended electron reservoir for efficient proton reduction in aqueous mediaSynthesis, Characterization, and Reactivity of Functionalized Trinuclear Iron-Sulfur Clusters - A New Class of Bioinspired Hydrogenase ModelsFrontiers, opportunities, and challenges in biochemical and chemical catalysis of CO2 fixationNitric oxide activation by distal redox modulation in tetranuclear iron nitrosyl complexesInfluence of the protein structure surrounding the active site on the catalytic activity of [NiFeSe] hydrogenases.Terminal vs bridging hydrides of diiron dithiolates: protonation of Fe2(dithiolate)(CO)2(PMe3)4.Water-assisted proton delivery and removal in bio-inspired hydrogen production catalysts.An electrochemical study of frustrated Lewis pairs: a metal-free route to hydrogen oxidationHydrogen 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 ComplexationCatalytic hydrogen oxidation: dawn of a new iron age.Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases.Connecting [NiFe]- and [FeFe]-hydrogenases: mixed-valence nickel-iron dithiolates with rotated structuresSynthetic models for the active site of the [FeFe]-hydrogenase: catalytic proton reduction and the structure of the doubly protonated intermediate.Diiron azadithiolates as models for the [FeFe]-hydrogenase active site and paradigm for the role of the second coordination sphereProton reduction to hydrogen in biological and chemical systems.Enzyme nanoarchitectonics: organization and device application.De novo design of functional proteins: Toward artificial hydrogenases.Structural and functional models in molybdenum and tungsten bioinorganic chemistry: description of selected model complexes, present scenario and possible future scopes.Heterogeneous catalysis and the challenges of powering the planet, securing chemicals for civilised life, and clean efficient utilization of renewable feedstocks.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.Electron transfer in dye-sensitised semiconductors modified with molecular cobalt catalysts: photoreduction of aqueous protons.Design, synthesis and characterization of a modular bridging ligand platform for bio-inspired hydrogen production.Nickel-centred proton reduction catalysis in a model of [NiFe] hydrogenase.Metal-free electrocatalytic hydrogen oxidation using frustrated Lewis pairs and carbon-based Lewis acids.Hydrogen activation by biomimetic [NiFe]-hydrogenase model containing protected cyanide cofactors.Chitosan confinement enhances hydrogen photogeneration from a mimic of the diiron subsite of [FeFe]-hydrogenase.Bridging-hydride influence on the electronic structure of an [FeFe] hydrogenase active-site model complex revealed by XAES-DFT.Biomimetic model for [FeFe]-hydrogenase: asymmetrically disubstituted diiron complex with a redox-active 2,2'-bipyridyl ligand.Arene non-innocence in dinuclear complexes of Fe, Co, and Ni supported by a para-terphenyl diphosphine.Access to Stable Metalloradical Cations with Unsupported and Isomeric Metal-Metal Hemi-Bonds.Synthetic Models for Nickel-Iron Hydrogenase Featuring Redox-Active Ligands.Synthesis and interconversions of reduced, alkali-metal supported iron-sulfur-carbonyl complexes.Influence of the Dithiolate Bridge on the Oxidative Processes of Diiron Models Related to the Active Site of [FeFe] Hydrogenases.An Unsaturated Four-Coordinate Dimethyl Dimolybdenum Complex with a Molybdenum-Molybdenum Quadruple Bond.A reversible proton relay process mediated by hydrogen-bonding interactions in [FeFe]hydrogenase modeling.
P2860
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P2860
Combining acid-base, redox and substrate binding functionalities to give a complete model for the [FeFe]-hydrogenase.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年学术文章
@wuu
2011年学术文章
@zh-cn
2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
@zh-sg
2011年學術文章
@yue
2011年學術文章
@zh
2011年學術文章
@zh-hant
name
Combining acid-base, redox and ...... el for the [FeFe]-hydrogenase.
@ast
Combining acid-base, redox and ...... el for the [FeFe]-hydrogenase.
@en
type
label
Combining acid-base, redox and ...... el for the [FeFe]-hydrogenase.
@ast
Combining acid-base, redox and ...... el for the [FeFe]-hydrogenase.
@en
prefLabel
Combining acid-base, redox and ...... el for the [FeFe]-hydrogenase.
@ast
Combining acid-base, redox and ...... el for the [FeFe]-hydrogenase.
@en
P2860
P356
P1433
P1476
Combining acid-base, redox and ...... el for the [FeFe]-hydrogenase.
@en
P2093
James M Camara
Thomas B Rauchfuss
P2860
P2888
P356
10.1038/NCHEM.1180
P577
2011-10-30T00:00:00Z