about
Genes required for rapid expression of nitrogenase activity in Azotobacter vinelandiiCatalytic reduction of dinitrogen to ammonia at a single molybdenum centerSmall RNA-induced differential degradation of the polycistronic mRNA iscRSUASubstrate pathways in the nitrogenase MoFe protein by experimental identification of small molecule binding sites.Structure of Precursor-Bound NifEN: A Nitrogenase FeMo Cofactor Maturase/InsertaseCharacterization of iron-sulfur protein assembly in isolated mitochondria. A requirement for ATP, NADH, and reduced iron.The yeast scaffold proteins Isu1p and Isu2p are required inside mitochondria for maturation of cytosolic Fe/S proteinsMechanism of Mo-dependent nitrogenaseThe structure and function of frataxin.Identification of a nitrogenase FeMo cofactor precursor on NifEN complex.Nitrogenase reactivity with P-cluster variants.Synthesis of diamidopyrrolyl molybdenum complexes relevant to reduction of dinitrogen to ammonia.Genetic regulation of biological nitrogen fixation.Adenosyl radical: reagent and catalyst in enzyme reactions.The Amt/Mep/Rh family of ammonium transport proteins.Azotobacter vinelandii vanadium nitrogenase: formaldehyde is a product of catalyzed HCN reduction, and excess ammonia arises directly from catalyzed azide reductionMitochondrial Protein Nfu1 Influences Homeostasis of Essential Metals in the Human Fungal Pathogen Cryptococcus neoformansModeling methanogenesis with a genome-scale metabolic reconstruction of Methanosarcina barkeri.Catalytic reduction of dinitrogen to ammonia at a single molybdenum center.A methyldiazene (HN=N-CH3)-derived species bound to the nitrogenase active-site FeMo cofactor: Implications for mechanismFlavodoxin hydroquinone reduces Azotobacter vinelandii Fe protein to the all-ferrous redox state with a S = 0 spin stateMiraculous catch of iron-sulfur protein sequences in the Sargasso Sea.Protein dynamics and the all-ferrous [Fe4 S4 ] cluster in the nitrogenase iron protein.Synthesis of [(HIPTNCH2CH2)3N]V compounds (HIPT = 3,5-(2,4,6-i-Pr3C6H2)2C6H3) and an evaluation of vanadium for the reduction of dinitrogen to ammonia.Synthesis of molybdenum complexes that contain "hybrid" triamidoamine ligands, [(hexaisopropylterphenyl-NCH2CH2)2NCH2CH2N-aryl]3-, and studies relevant to catalytic reduction of dinitrogen.X-ray Absorption and Emission Spectroscopic Studies of [L2Fe2S2](n) Model Complexes: Implications for the Experimental Evaluation of Redox States in Iron-Sulfur Clusters.Nitrogenase FeMo cofactor: an atomic structure in three simple steps.Biosynthesis of (bacterio)chlorophylls: ATP-dependent transient subunit interaction and electron transfer of dark operative protochlorophyllide oxidoreductase.Identification of three genes encoding P(II)-like proteins in Gluconacetobacter diazotrophicus: studies of their role(s) in the control of nitrogen fixation.2-Oxoglutarate:NADP(+) oxidoreductase in Azoarcus evansii: properties and function in electron transfer reactions in aromatic ring reduction.Glutamine synthetase stabilizes the binding of GlnR to nitrogen fixation gene operators.Nitrogen-Fixing Nodules Are an Important Source of Reduced Sulfur, Which Triggers Global Changes in Sulfur Metabolism in Lotus japonicus.Gas exchange in the filamentous cyanobacterium Nostoc punctiforme strain ATCC 29133 and Its hydrogenase-deficient mutant strain NHM5.Effects of disruption of homocitrate synthase genes on Nostoc sp. strain PCC 7120 photobiological hydrogen production and nitrogenase.A new small regulatory protein, HmuP, modulates haemin acquisition in Sinorhizobium meliloti13C NMR characterization of an exchange reaction between CO and CO2 catalyzed by carbon monoxide dehydrogenase.Expression, purification and crystallization of the ammonium transporter Amt-1 from Archaeoglobus fulgidus.A molecular pathway for the egress of ammonia produced by nitrogenase.The [Fe-Fe]-hydrogenase maturation protein HydF from Thermotoga maritima is a GTPase with an iron-sulfur cluster.Genetic differentiation of Trifolium repens microsymbionts deriving from Zn-Pb waste-heap and control area in Poland.
P2860
Q24524115-4D2BD2EF-2D2E-472A-AEBE-4E4EC4D5E4A2Q24645184-62E13F6B-5C0B-4B8A-8E55-AC234112B96FQ24649054-DE7D3E30-1F88-4028-982B-9CC36313E653Q27339663-61544F9E-A6B9-45AC-9B30-B3CEE1347FFBQ27666506-7A89ED9E-3DDD-45B1-A96F-AB78CC084CF8Q27936228-0EEED254-775E-4BF2-BB98-44F25AB51BDCQ27937038-2F24E174-2937-475D-A54A-BA7BF937FAFBQ33622954-2B7DC7CB-CDFF-450D-828F-F75AE79FC15CQ33808205-281B351D-6521-4A52-816B-CB1432709A4EQ33927504-ABD84960-B3BD-49BA-9EC8-A8DC9D8BA6A2Q34048250-D2AB9BAA-513E-412C-A175-0DCD462351F6Q34097183-33AEF472-987E-4EEF-901B-E014EEA18A4BQ34334558-9B45E46D-8236-496E-815A-71C50B633744Q34447149-04705013-44E2-451F-922B-036F1691542DQ34665528-1CEF4FE9-3C87-42E8-8DD8-D46DAE379AC7Q34976809-E4D32730-070D-4A41-A00C-65C80F6CE4CBQ34984235-81AB4782-329D-44AD-9B4C-2FE08BCABB4DQ35193476-39D52755-669A-433A-A79B-C16BFCC32C54Q35215172-29514C47-31EB-4035-BA62-E8EC85A8179FQ35215180-F6C760E8-088F-42CF-B50E-36B4BAB38BD5Q35768465-2A5AF2B6-EB31-4A3F-8DAC-383B5BA7EC91Q35835136-C706688F-AAE5-4E53-BF08-4655C20BEDB4Q36749506-E1DCC695-6607-4FF8-8487-5FEB37C9DF9CQ36853481-AB6FDD0F-412C-4EA9-808F-2AD1A5291BF7Q37002500-CBA60A22-7414-4698-A85C-7445C3C17BF7Q37413045-09FFF739-0591-47F8-8E1F-032A443DE463Q38190030-CD720EDD-0412-45BD-A022-C05C9FE81EE6Q39431581-A0036E74-C60F-4078-B614-AAB84CC70006Q39887775-C248B1E6-21D7-4338-9BBC-46DACC7E09E1Q39997751-A8271F47-1B86-470C-B8B4-B57C7C965D23Q40363353-7AB55EAC-AC40-490D-B5BB-B269AE11384DQ40618299-25FDC5D8-DD6A-4EBA-A45C-43655DB995D8Q40743896-79BEF64B-04DE-4245-A1E4-8D08FA517527Q41773261-AF292ED0-C9E2-4406-8AA7-A4DDEF59610BQ41973625-B864D616-DD20-4FB6-A226-08385970566CQ42116348-2CDD5581-571B-4A45-9AA3-03FA72810923Q42371051-24002786-F895-49D6-B1C9-45277B71B4E4Q42883526-2832244E-8A24-48AF-9D0A-5BBC95A2D7F0Q43018711-2C16EE42-6582-4091-AF68-6E0B0D991153Q43325309-5ADCD880-ED33-4B0D-AFDE-AF19CEE3BDD5
P2860
description
2000 nî lūn-bûn
@nan
2000 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Nitrogenase: standing at the crossroads.
@ast
Nitrogenase: standing at the crossroads.
@en
Nitrogenase: standing at the crossroads.
@nl
type
label
Nitrogenase: standing at the crossroads.
@ast
Nitrogenase: standing at the crossroads.
@en
Nitrogenase: standing at the crossroads.
@nl
prefLabel
Nitrogenase: standing at the crossroads.
@ast
Nitrogenase: standing at the crossroads.
@en
Nitrogenase: standing at the crossroads.
@nl
P1476
Nitrogenase: standing at the crossroads.
@en
P2093
P304
P356
10.1016/S1367-5931(00)00132-0
P577
2000-10-01T00:00:00Z