Chelate control of diiron(I) dithiolates relevant to the [Fe-Fe]- hydrogenase active site - Wikidata - wikimedia - TriplyDB

Chelate control of diiron(I) dithiolates relevant to the [Fe-Fe]- hydrogenase active site

Chelate control of diiron(I) dithiolates relevant to the [Fe-Fe]- hydrogenase active site

http://www.wikidata.org/entity/Q36726929

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The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site Terminal vs bridging hydrides of diiron dithiolates: protonation of Fe2(dithiolate)(CO)2(PMe3)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 Hydrogen Production Catalyzed by Bidirectional, Biomimetic Models of the [FeFe]-Hydrogenase Active Site.EPR/ENDOR, Mössbauer, and quantum-chemical investigations of diiron complexes mimicking the active oxidized state of [FeFe]hydrogenase.Reaction of Aryl Diazonium Salts and Diiron(I) Dithiolato Carbonyls: Evidence for Radical Intermediates.Combining acid-base, redox and substrate binding functionalities to give a complete model for the [FeFe]-hydrogenase.Isomerization of the hydride complexes [HFe2(SR)2(PR3)(x)(CO)(6-x)]+ (x = 2, 3, 4) relevant to the active site models for the [FeFe]-hydrogenases 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.Synthetic 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 sphere Terminal hydride in [FeFe]-hydrogenase model has lower potential for H2 production than the isomeric bridging hydride.Unsaturated, mixed-valence diiron dithiolate model for the H(ox) state of the [FeFe] hydrogenase Nitrosyl derivatives of diiron(I) dithiolates mimic the structure and Lewis acidity of the [FeFe]-hydrogenase active site.New nitrosyl derivatives of diiron dithiolates related to the active site of the [FeFe]-hydrogenases.Ferrous Carbonyl Dithiolates as Precursors to FeFe, FeCo, and FeMn Carbonyl Dithiolates.De novo design of functional proteins: Toward artificial hydrogenases.Bioinspired Hydrogenase Models: The Mixed-Valence Triiron Complex [Fe3(CO)7(μ-edt)2] and Phosphine Derivatives [Fe3(CO)7-x (PPh3) x (μ-edt)2] (x = 1, 2) and [Fe3(CO)5(κ(2)-diphosphine)(μ-edt)2] as Proton Reduction Catalysts.Desymmetrized Diiron Azadithiolato Carbonyls: A Step Toward Modeling the Iron-Only Hydrogenases.Models of the iron-only hydrogenase: a comparison of chelate and bridge isomers of Fe2(CO)4{Ph2PN(R)PPh2}(μ-pdt) as proton-reduction catalysts.Role of the azadithiolate cofactor in models for [FeFe]-hydrogenase: novel structures and catalytic implications Hydride-containing models for the active site of the nickel-iron hydrogenases.Redox and structural properties of mixed-valence models for the active site of the [FeFe]-hydrogenase: progress and challenges.Mild redox complementation enables H2 activation by [FeFe]-hydrogenase models.Electronic and geometric effects of phosphatriazaadamantane ligands on the catalytic activity of an [FeFe] hydrogenase inspired complex.Precursors to [FeFe]-hydrogenase models: syntheses of Fe2(SR)2(CO)6 from CO-free iron sources.Crystallographic characterization of a fully rotated, basic diiron dithiolate: model for the H(red) state?Biomimetic model for [FeFe]-hydrogenase: asymmetrically disubstituted diiron complex with a redox-active 2,2'-bipyridyl ligand.Isolation, observation, and computational modeling of proposed intermediates in catalytic proton reductions with the hydrogenase mimic Fe2(CO)6S2C6H4.Protonation/reduction dynamics at the [4Fe-4S] cluster of the hydrogen-forming cofactor in [FeFe]-hydrogenases.{AsW9O33}-{Mo3S4} based polyoxometalates including a metal-metal bond with Pd or Ni. Synthesis, structure and studies in solution.

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P2860

Chelate control of diiron(I) dithiolates relevant to the [Fe-Fe]- hydrogenase active site

http://www.wikidata.org/entity/Q36726929

description

2007 nî lūn-bûn

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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2007年论文

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name

Chelate control of diiron(I) dithiolates relevant to the [Fe-Fe]- hydrogenase active site

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Chelate control of diiron(I) dithiolates relevant to the [Fe-Fe]- hydrogenase active site

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Chelate control of diiron(I) dithiolates relevant to the [Fe-Fe]- hydrogenase active site

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Chelate control of diiron(I) dithiolates relevant to the [Fe-Fe]- hydrogenase active site

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Chelate control of diiron(I) dithiolates relevant to the [Fe-Fe]- hydrogenase active site

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Chelate control of diiron(I) dithiolates relevant to the [Fe-Fe]- hydrogenase active site

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Inorganic Chemistry

P1476

Chelate control of diiron(I) dithiolates relevant to the [Fe-Fe]- hydrogenase active site

@en

P2093

Aaron K Justice

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

Jarl Ivar van der Vlugt

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Luca De Gioia

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Scott R Wilson

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Thomas B Rauchfuss

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P2860

Density-functional exchange-energy approximation with correct asymptotic behavior

Density-functional approximation for the correlation energy of the inhomogeneous electron gas

Hydrogenases: hydrogen-activating enzymes.

Better than platinum? Fuel cells energized by enzymes.

Coordination sphere flexibility of active-site models for Fe-only hydrogenase: studies in intra- and intermolecular diatomic ligand exchange.

Density functional theory investigation of the active site of Fe-hydrogenases. systematic study of the effects of redox state and ligands hardness on structural and electronic properties of complexes related to the [2Fe](H) subcluster.

[Fe2(SR)2(mu-CO)(CNMe)6]2+ and analogues: a new class of diiron dithiolates as structural models for the H(ox)Air state of the fe-only hydrogenase.

Dissecting the intimate mechanism of cyanation of {2Fe3S} complexes related to the active site of all-iron hydrogenases by DFT analysis of energetics, transition states, intermediates and products in the carbonyl substitution pathway.

Electron-rich diferrous-phosphane-thiolates relevant to Fe-only hydrogenase: is cyanide "nature's trimethylphosphane"?

P304

1655-1664

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scholarly article

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10.1021/IC0618706

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P433

5

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46

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Giuseppe Zampella

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2007-02-06T00:00:00Z

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6524488

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17279743

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2430879

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