Trapping H- bound to the nitrogenase FeMo-cofactor active site during H2 evolution: characterization by ENDOR spectroscopy.
about
How many metals does it take to fix N2? A mechanistic overview of biological nitrogen fixationMechanism of nitrogen fixation by nitrogenase: the next stageTurnover-Dependent Inactivation of the Nitrogenase MoFe-Protein at High pHLow frequency dynamics of the nitrogenase MoFe protein via femtosecond pump probe spectroscopy - Observation of a candidate promoting vibrationCarbon dioxide reduction to methane and coupling with acetylene to form propylene catalyzed by remodeled nitrogenaseNitrogenase: a draft mechanismOn reversible H2 loss upon N2 binding to FeMo-cofactor of nitrogenase.Mechanism of Mo-dependent nitrogenaseTrapping an intermediate of dinitrogen (N2) reduction on nitrogenaseA substrate channel in the nitrogenase MoFe protein.Insight into the Iron-Molybdenum Cofactor of Nitrogenase from Synthetic Iron Complexes with Sulfur, Carbon, and Hydride Ligands57Fe ENDOR spectroscopy and 'electron inventory' analysis of the nitrogenase E4 intermediate suggest the metal-ion core of FeMo-cofactor cycles through only one redox coupleConnecting nitrogenase intermediates with the kinetic scheme for N2 reduction by a relaxation protocol and identification of the N2 binding state.On the feasibility of N2 fixation via a single-site FeI/FeIV cycle: Spectroscopic studies of FeI(N2)FeI, FeIV[triple bond]N, and related speciesA methyldiazene (HN=N-CH3)-derived species bound to the nitrogenase active-site FeMo cofactor: Implications for mechanismAdvanced paramagnetic resonance spectroscopies of iron-sulfur proteins: Electron nuclear double resonance (ENDOR) and electron spin echo envelope modulation (ESEEM)Electron transfer in nitrogenase catalysis.Synthesis, Characterization, and Nitrogenase-Relevant Reactions of an Iron Sulfide Complex with a Bridging Hydride.The reactivity patterns of low-coordinate iron-hydride complexes.Mechanistic insight into N=N cleavage by a low-coordinate iron(II) hydride complexNitrogenase reduction of carbon-containing compounds.Characterization of the Fe-H bond in a three-coordinate terminal hydride complex of iron(I).Climbing nitrogenase: toward a mechanism of enzymatic nitrogen fixation.Synthesis, spectroscopy, and hydrogen/deuterium exchange in high-spin iron(II) hydride complexesNitrogenase FeMo cofactor: an atomic structure in three simple steps.Synthesis and Mechanism of Formation of Hydride-Sulfide Complexes of Iron.Reversible Photoinduced Reductive Elimination of H2 from the Nitrogenase Dihydride State, the E(4)(4H) Janus Intermediate.A confirmation of the quench-cryoannealing relaxation protocol for identifying reduction states of freeze-trapped nitrogenase intermediates.Hydrogenase Enzymes and Their Synthetic Models: The Role of Metal Hydrides.Nitrogenase Cofactor: Inspiration for Model Chemistry.Is Mo involved in hydride binding by the four-electron reduced (E4) intermediate of the nitrogenase MoFe protein?Formation of {[HIPTN(3)N]Mo(III)H}(-) by heterolytic cleavage of H(2) as established by EPR and ENDOR spectroscopy.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 ComplexCO2 Reduction Catalyzed by Nitrogenase: Pathways to Formate, Carbon Monoxide, and Methane.Modeling the signatures of hydrides in metalloenzymes: ENDOR analysis of a Di-iron Fe(μ-NH)(μ-H)Fe core.ENDOR/HYSCORE studies of the common intermediate trapped during nitrogenase reduction of N2H2, CH3N2H, and N2H4 support an alternating reaction pathway for N2 reductionCatalytic transformation of dinitrogen into ammonia and hydrazine by iron-dinitrogen complexes bearing pincer ligand.Borane B-C Bond Cleavage by a Low-Coordinate Iron Hydride Complex and N-N Bond Cleavage by the Hydridoborate Product.A 10(6)-fold enhancement in N2-binding affinity of an Fe2(μ-H)2 core upon reduction to a mixed-valence Fe(II)Fe(I) state.
P2860
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P2860
Trapping H- bound to the nitrogenase FeMo-cofactor active site during H2 evolution: characterization by ENDOR spectroscopy.
description
2005 nî lūn-bûn
@nan
2005 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Trapping H- bound to the nitro ...... ization by ENDOR spectroscopy.
@ast
Trapping H- bound to the nitro ...... ization by ENDOR spectroscopy.
@en
Trapping H- bound to the nitro ...... ization by ENDOR spectroscopy.
@nl
type
label
Trapping H- bound to the nitro ...... ization by ENDOR spectroscopy.
@ast
Trapping H- bound to the nitro ...... ization by ENDOR spectroscopy.
@en
Trapping H- bound to the nitro ...... ization by ENDOR spectroscopy.
@nl
prefLabel
Trapping H- bound to the nitro ...... ization by ENDOR spectroscopy.
@ast
Trapping H- bound to the nitro ...... ization by ENDOR spectroscopy.
@en
Trapping H- bound to the nitro ...... ization by ENDOR spectroscopy.
@nl
P2093
P356
P1476
Trapping H- bound to the nitro ...... ization by ENDOR spectroscopy.
@en
P2093
Brian M Hoffman
Dennis R Dean
Hong-In Lee
Lance C Seefeldt
Mikhail Laryukhin
Patricia C Dos Santos
Robert Y Igarashi
P304
P356
10.1021/JA043596P
P407
P577
2005-05-01T00:00:00Z