Is Mo involved in hydride binding by the four-electron reduced (E4) intermediate of the nitrogenase MoFe protein?
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Mechanism of nitrogen fixation by nitrogenase: the next stageCarbon 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.Reactivity of hydride bridges in a high-spin [Fe3(μ-H)3]3+ cluster: reversible H2/CO exchange and Fe-H/B-F bond metathesisInsight 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 coupleLight-driven dinitrogen reduction catalyzed by a CdS:nitrogenase MoFe protein biohybrid.Steric control of the Hi-CO MoFe nitrogenase complex revealed by stopped-flow infrared spectroscopyAdvanced paramagnetic resonance spectroscopies of iron-sulfur proteins: Electron nuclear double resonance (ENDOR) and electron spin echo envelope modulation (ESEEM)Unification of reaction pathway and kinetic scheme for N2 reduction catalyzed by nitrogenaseElectron transfer in nitrogenase catalysis.EXAFS and NRVS reveal a conformational distortion of the FeMo-cofactor in the MoFe nitrogenase propargyl alcohol complex.Nitrogenase reduction of carbon-containing compounds.Characterization of the Fe-H bond in a three-coordinate terminal hydride complex of iron(I).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.Molybdenum L-Edge XAS Spectra of MoFe Nitrogenase.Reductive Elimination of H2 Activates Nitrogenase to Reduce the N≡N Triple Bond: Characterization of the E4(4H) Janus Intermediate in Wild-Type Enzyme.Exploring Electron/Proton Transfer and Conformational Changes in the Nitrogenase MoFe Protein and FeMo-cofactor Through Cryoreduction/EPR Measurements.Modeling the signatures of hydrides in metalloenzymes: ENDOR analysis of a Di-iron Fe(μ-NH)(μ-H)Fe core.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.Identification of a key catalytic intermediate demonstrates that nitrogenase is activated by the reversible exchange of N₂ for H₂.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.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?Hydride Conformers of the Nitrogenase FeMo-cofactor Two-Electron Reduced State E2(2H), Assigned Using Cryogenic Intra Electron Paramagnetic Resonance Cavity Photolysis.N2Binding to the FeMo-Cofactor of NitrogenaseIdentification of a spin-coupled Mo(iii) in the nitrogenase iron–molybdenum cofactor
P2860
Q26828626-78013ABB-1EAD-476C-ADFA-BE6B0744FF00Q28710446-80EA6C12-E00C-4B08-8866-A54836E5A27FQ33354977-434AC103-5FB3-4A78-AD9D-AD5F943DF100Q33356598-C4D1151C-25CE-418B-842E-9F09E2F4BB18Q33726092-00E120ED-7518-4D3A-B71E-127458911AD1Q33899998-7911CD7C-26CD-48C5-88DA-906694CBB2CEQ34222221-2F45911E-67B4-4558-B968-5460C5368730Q34523075-92945E2F-5285-4A82-8829-210ECC7322F5Q35217536-32F74F42-3AF2-42F2-A933-E7F450D313D5Q35329323-C11D3B7F-87F9-4BE9-BB1D-8C7CCA4FCFC6Q35889412-DDA62F79-7399-45B2-829D-2668866AA37DQ35894679-84B03B71-2D53-41AF-8DB8-A61AC3D6A8E4Q36007696-BD0ECD6B-BE18-40B0-B119-7A841C8CA029Q37022097-B211094D-E9D2-466B-B904-F3128049258FQ37086641-CBB8F9EE-FEF7-4644-BCFE-EB7AE5FC4BE8Q38700898-935EDC1E-AFC3-46DB-BB3C-52D83F559A02Q38862091-0BAC447F-E947-496F-A7ED-47C75AC1417CQ40693660-E3324B77-9150-4889-9E8F-8774F815D082Q41100357-0D891AFD-1F1B-40D5-BB3D-99D37AF8E528Q41644842-44B6C73A-922A-4984-9C92-FA9C63CA7826Q41761954-0FADA5C4-F2F3-4531-A838-E21ED211A2DAQ42547488-7AF31F07-DFFA-4A67-A323-E26B64D5065CQ42553068-5770DC2A-5BA8-4A29-B899-4F0443807991Q45052374-98F50B7C-6DAE-4058-9400-86F09855909CQ45066199-DA4E8BD8-48C8-4315-B9DC-C4541F2BC3FDQ46457734-C63244D7-8AAE-48A9-8D2A-9A89A865D153Q47249714-B2D7000A-698F-4FF7-9980-D5904AF406CFQ48371676-2B32E520-F346-4AA8-B66B-4AE5550D080EQ55278759-99111ABB-FF64-4483-8C57-C1CD63F7B5F9Q55982942-1A8233BB-DABC-4005-9603-41896361623CQ58009574-53FB6E0A-EC95-49E7-94E5-CF264BEB608A
P2860
Is Mo involved in hydride binding by the four-electron reduced (E4) intermediate of the nitrogenase MoFe protein?
description
2010 nî lūn-bûn
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2010年の論文
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年学术文章
@zh-my
2010年学术文章
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2010年學術文章
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name
Is Mo involved in hydride bind ...... the nitrogenase MoFe protein?
@en
Is Mo involved in hydride binding by the four-electron reduced
@nl
type
label
Is Mo involved in hydride bind ...... the nitrogenase MoFe protein?
@en
Is Mo involved in hydride binding by the four-electron reduced
@nl
prefLabel
Is Mo involved in hydride bind ...... the nitrogenase MoFe protein?
@en
Is Mo involved in hydride binding by the four-electron reduced
@nl
P2093
P2860
P356
P1476
Is Mo involved in hydride bind ...... the nitrogenase MoFe protein?
@en
P2093
Brian M Hoffman
Dennis R Dean
Dmitriy Lukoyanov
Lance C Seefeldt
Zhi-Yong Yang
P2860
P304
P356
10.1021/JA910613M
P407
P577
2010-03-01T00:00:00Z