Unique features of the nitrogenase VFe protein from Azotobacter vinelandii.
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Mechanism of nitrogen fixation by nitrogenase: the next stageCharacterization of isolated nitrogenase FeVcoThe Structural Basis of Action of Vanadyl (VO(2+)) Chelates in Cells.Regulation of Three Nitrogenase Gene Clusters in the Cyanobacterium Anabaena variabilis ATCC 29413Nitrogenase and homologs.Structural models of the [Fe4S4] clusters of homologous nitrogenase Fe proteinsExtending the carbon chain: hydrocarbon formation catalyzed by vanadium/molybdenum nitrogenasesUncoupling binding of substrate CO from turnover by vanadium nitrogenase.Widening the Product Profile of Carbon Dioxide Reduction by Vanadium Nitrogenase.Classifying the metal dependence of uncharacterized nitrogenases.Vanadium nitrogenase: a two-hit wonder?Comparative electronic structures of nitrogenase FeMoco and FeVco.Production and isolation of vanadium nitrogenase from Azotobacter vinelandii by molybdenum depletion.Differential reduction of CO₂ by molybdenum and vanadium nitrogenases.Activation of CO2 by Vanadium Nitrogenase.The in vivo hydrocarbon formation by vanadium nitrogenase follows a secondary metabolic pathway.Catalytic reduction of CN-, CO, and CO2 by nitrogenase cofactors in lanthanide-driven reactions.NifA- and CooA-coordinated cowN expression sustains nitrogen fixation by Rhodobacter capsulatus in the presence of carbon monoxide.The Fe-V Cofactor of Vanadium Nitrogenase Contains an Interstitial Carbon Atom.Production of polyhydroxybutyrate and alginate from glycerol by Azotobacter vinelandii under nitrogen-free conditions.ATP-independent formation of hydrocarbons catalyzed by isolated nitrogenase cofactorsInsights into hydrocarbon formation by nitrogenase cofactor homologs.Tracing the hydrogen source of hydrocarbons formed by vanadium nitrogenase.Regulation of V-nitrogenase genes in Anabaena variabilis by RNA processing and by dual repressors.Activation and reduction of carbon dioxide by nitrogenase iron proteins.Effect of nitric oxide on VnfA, a transcriptional activator of VFe-nitrogenase in Azotobacter vinelandii.The Mechanism of N2 Reduction Catalyzed by Fe-Nitrogenase Involves Reductive Elimination of H2.The structure of vanadium nitrogenase reveals an unusual bridging ligand.Characterization of an M-Cluster-Substituted Nitrogenase VFe Protein.ATP-dependent substrate reduction at an [Fe8S9] double-cubane cluster.
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P2860
Unique features of the nitrogenase VFe protein from Azotobacter vinelandii.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 28 May 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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Unique features of the nitrogenase VFe protein from Azotobacter vinelandii.
@en
Unique features of the nitrogenase VFe protein from Azotobacter vinelandii.
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type
label
Unique features of the nitrogenase VFe protein from Azotobacter vinelandii.
@en
Unique features of the nitrogenase VFe protein from Azotobacter vinelandii.
@nl
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Unique features of the nitrogenase VFe protein from Azotobacter vinelandii.
@en
Unique features of the nitrogenase VFe protein from Azotobacter vinelandii.
@nl
P2093
P2860
P356
P1476
Unique features of the nitrogenase VFe protein from Azotobacter vinelandii.
@en
P2093
Chi Chung Lee
Markus W Ribbe
P2860
P304
P356
10.1073/PNAS.0904408106
P407
P577
2009-05-28T00:00:00Z