Trapping H- bound to the nitrogenase FeMo-cofactor active site during H2 evolution: characterization by ENDOR spectroscopy. - Wikidata - awgldk - TriplyDB

Trapping H- bound to the nitrogenase FeMo-cofactor active site during H2 evolution: characterization by ENDOR spectroscopy.

Trapping H- bound to the nitrogenase FeMo-cofactor active site during H2 evolution: characterization by ENDOR spectroscopy.

http://www.wikidata.org/entity/Q34413857

about

How many metals does it take to fix N2? A mechanistic overview of biological nitrogen fixation Mechanism of nitrogen fixation by nitrogenase: the next stage Turnover-Dependent Inactivation of the Nitrogenase MoFe-Protein at High pH Low frequency dynamics of the nitrogenase MoFe protein via femtosecond pump probe spectroscopy - Observation of a candidate promoting vibration Carbon dioxide reduction to methane and coupling with acetylene to form propylene catalyzed by remodeled nitrogenase Nitrogenase: a draft mechanism On reversible H2 loss upon N2 binding to FeMo-cofactor of nitrogenase.Mechanism of Mo-dependent nitrogenase Trapping an intermediate of dinitrogen (N2) reduction on nitrogenase A substrate channel in the nitrogenase MoFe protein.Insight into the Iron-Molybdenum Cofactor of Nitrogenase from Synthetic Iron Complexes with Sulfur, Carbon, and Hydride Ligands 57Fe ENDOR spectroscopy and 'electron inventory' analysis of the nitrogenase E4 intermediate suggest the metal-ion core of FeMo-cofactor cycles through only one redox couple Connecting 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 species A methyldiazene (HN=N-CH3)-derived species bound to the nitrogenase active-site FeMo cofactor: Implications for mechanism Advanced 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 complex Nitrogenase 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 complexes Nitrogenase 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 Complex CO2 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 reduction Catalytic 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

Q24676933-D8773087-545C-47FF-8ED9-A56458F35C57 Q26828626-C38E70DA-E677-4A84-A200-C14676055CEA Q27681203-EDED800E-A2FB-4714-A0A1-765F1D572CD6 Q28600846-EADB041A-D35B-4410-A52E-E77565B42F13 Q28710446-75A528DA-E1D5-4780-B000-C0F594DCB3C8 Q33354977-4FBCFDB7-BD85-4104-9E85-F11CF61804F5 Q33356598-2AC0EB85-ECFE-4190-9FAD-02BE9E6ECE87 Q33622954-C7478ED9-A955-42B2-8118-38AD8943DCCB Q33623026-DF434B06-F115-429A-8B8E-4958C16A64AC Q33641473-B13B30BC-276F-4D2E-A17A-0C78DA667870 Q33899998-062E0E34-EDFE-401B-BED9-5DA05361E002 Q34222221-81D7C891-72D4-46CD-BE0D-A788B7ED63F6 Q34605923-95277230-5281-4F8A-BC96-81E76F2B400A Q35215175-D0762B09-0026-4597-BCAD-AD53E80693F9 Q35215180-C819B5C7-DEC5-4024-A38C-514656A475DE Q35329323-40370E72-3A27-4BCA-9FDE-BE7CD0E23CEF Q35894679-7F7CD5BC-4E7D-4945-8835-6DFECD64703E Q36757271-E7488432-72EF-464A-AEB6-61F3385CA45C Q36776461-6E14BF00-C120-4D9F-890A-2AEC74EB7956 Q36901523-224E7647-1FEE-42A4-90D2-1CF494515489 Q37022097-44A01462-5665-4189-8EFE-49E0104CCC0A Q37086641-55F7842E-E4D8-4FB2-9FCE-97A5BE9E38C8 Q37198257-E2ACF6E7-1C59-4675-BB65-8ECB6D0A9218 Q37714205-4011F9DD-6611-42B7-93D4-867133DBDD30 Q38190030-E6AAE5C9-B0F9-4704-ACEF-A39862EA205F Q38670824-62EF9489-3CFB-4739-B10D-75272742062D Q38700898-A0749BB8-B3D3-45CF-A0A7-BAA9C9A74481 Q38862091-74638CCE-17CF-4EC0-8AFE-EA8863B82F8A Q38880043-AAC0A47F-57D3-4FF6-9007-388BFF32F5D9 Q39251558-F650D19E-C6F4-44AE-A449-E673B627DBF2 Q39272554-5175E9F7-E905-41D3-9810-F38AB04D1F9C Q39778098-B1821F2D-6D09-4397-BFFE-AE5E2D2DFB06 Q41100357-FEB707E0-942B-45E7-82C6-A3D6BE6C8290 Q41333969-B1261704-19A0-4829-B51D-780AEC0E4F75 Q41489932-DFEB07F4-BF0B-4CE9-B974-6384B529446E Q41761954-E133560F-9BBA-41D3-8E2E-589D5C0BE98B Q41886086-D053D45B-1E35-4ABB-80E4-9832C8B382A4 Q42402359-5987AF2B-FE0B-45C8-AD25-AD80F9F036FB Q42404282-4C0D9032-9C53-4CE1-A07C-BD4BD4A62D20 Q42547488-BB6741B5-8C8A-4961-881D-4BB02F3A47BF

P2860

Trapping H- bound to the nitrogenase FeMo-cofactor active site during H2 evolution: characterization by ENDOR spectroscopy.

http://www.wikidata.org/entity/Q34413857

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

P1433

Q34413857-B2F35D15-7E77-4D83-8B5B-3ABB51CF7C28

P1476

Q34413857-362CDCC9-2202-462D-9A3B-C885838A284D

P2093

Q34413857-006F83D9-5305-410F-9640-3030FC9124A7

Q34413857-1DA93576-B64A-46F4-9251-4F5EA99D9E5A

Q34413857-47633213-CE44-449B-9D26-D4FB9DE7D2C9

Q34413857-81B85C9C-6BBF-4036-87BD-E457B4A27068

Q34413857-939F4BFF-194F-4AF2-A167-E8B70A736407

Q34413857-C9DDB423-F6A5-456B-89C5-47661F091655

Q34413857-F83A760B-3310-4710-8AB2-C5451FD1A203

P304

Q34413857-0C33C58D-9DA7-4016-8DFA-6B9F3A9B8BE8

P31

Q34413857-424F0A2D-31E3-499E-B8B4-C3ED5BAD1F9F

P356

Q34413857-2023D4EE-A1D2-487E-9B48-A06AE50DAD1C

P407

Q34413857-D990DCDF-D4B1-4BE0-BC0A-2D77099701E8

P433

Q34413857-09F41F23-407D-41F3-BD35-2C9F9AAE7E55

P478

Q34413857-724FD0D2-6FE0-4063-A374-E48C5639F85E

P577

Q34413857-A7C66E03-13CE-427F-B966-F695801267C6

P698

Q34413857-89EB215F-DBD0-4351-B456-7AB24E8C87C2

P356

P1433

Journal of the American Chemical Society

P1476

Trapping H- bound to the nitro ...... ization by ENDOR spectroscopy.

@en

P2093

Brian M Hoffman

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

Dennis R Dean

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

Hong-In Lee

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

Lance C Seefeldt

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

Mikhail Laryukhin

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

Patricia C Dos Santos

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

Robert Y Igarashi

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

P304

6231-6241

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

P31

scholarly article

P356

10.1021/JA043596P

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

P407

P433

17

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

P478

127

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

P577

2005-05-01T00:00:00Z

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

P698

15853328

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