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Structure−Function Relationships of Alternative Nitrogenases

https://doi.org/10.1021/cr950057h
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/j.1460-2075.1989.tb03495.xopenalex-snapshot
Structural genes for the vanadium nitrogenase from Azotobacter chroococcum.
inferredcites →https://doi.org/10.1007/978-1-4684-7609-5_5openalex-snapshot
Ribosomal RNA Analysis of Microorganisms as They Occur in Nature
inferredcites →https://doi.org/10.1007/978-1-4684-8523-3_2openalex-snapshot
Reactions and Physicochemical Properties of the Nitrogenase Mofe Proteins
inferredcites →https://doi.org/10.1007/978-94-017-2416-6_10openalex-snapshot
The Crystal Structure of the Nitrogenase MoFe Protein from Clostridium Pasteurianum
inferredcites →https://doi.org/10.1007/978-94-017-2416-6_15openalex-snapshot
Metal Regulation of Nitrogenases and Molybdenum Transport in Azotobacter Vinelandii
inferredcites →https://doi.org/10.1007/978-94-017-2416-6_2openalex-snapshot
Nitrogenases: Distribution, Composition, Structure and Function
inferredcites →https://doi.org/10.1007/978-94-017-2416-6_5openalex-snapshot
Organization and Regulation of Nitrogen Fixation Genes
inferredcites →https://doi.org/10.1007/bf00292722openalex-snapshot
The nifU, nifS and nifV gene products are required for activity of all three nitrogenases of Azotobacter vinelandii
inferredcites →https://doi.org/10.1007/bf00430445openalex-snapshot
The nifH, nifM and nifN genes of Azotobacter vinelandii: Characterisation by Tn5 mutagenesis and isolation from pLAFR1 gene banks
inferredcites →https://doi.org/10.1007/bf01132694openalex-snapshot
Rapid purification of the protein components of a highly active ?iron only? nitrogenase
inferredcites →https://doi.org/10.1016/0003-2697(92)90491-oopenalex-snapshot
Correction for creatine interference with the direct indophenol measurement of NH3 in steady-state nitrogenase assays
inferredcites →https://doi.org/10.1016/0005-2795(80)90015-xopenalex-snapshot
Nitrogenase XII. Mössbauer studies of the MoFe protein from Clostridium pasteurianum W5
inferredcites →https://doi.org/10.1016/0006-291x(70)90557-7openalex-snapshot
A vanadium containing nitrogenase preparation: Implications for the role of molybdenum in nitrogen fixation
inferredcites →https://doi.org/10.1016/0006-291x(71)90377-9openalex-snapshot
Nitrogenase from vanadium-grown : Isolation, characteristics, and mechanistic implications
inferredcites →https://doi.org/10.1016/0014-5793(92)80472-sopenalex-snapshot
EPR spectroscopic characterization of an ‘iron only⌉ nitrogenase S = 3/2 spectrum of component 1 isolated from Rhodobacter capsulatus
inferredcites →https://doi.org/10.1016/0162-0134(95)97646-8openalex-snapshot
Characterization of the “iron only” nitrogenase from Rhodobacter capsulatus
inferredcites →https://doi.org/10.1016/0162-0134(95)97654-9openalex-snapshot
Modification of the properties of nitrogenase P-clusters via site-directed mutagenesis of coordinating residues
inferredcites →https://doi.org/10.1016/0167-4781(93)90096-vopenalex-snapshot
Organization of potential alternative nitrogenase genes from Clostridium pasteurianum
inferredcites →https://doi.org/10.1016/0304-4165(72)90113-4openalex-snapshot
The vanadium effect in nitrogen fixation by azotobacter
inferredcites →https://doi.org/10.1016/s0021-9258(17)31909-9openalex-snapshot
Mössbauer characterization of the metal clusters in Azotobacter vinelandii nitrogenase VFe protein.
inferredcites →https://doi.org/10.1016/s0021-9258(17)32225-1openalex-snapshot
Catalytic formation of a nitrogenase iron-sulfur cluster.
inferredcites →https://doi.org/10.1016/s0021-9258(17)42235-6openalex-snapshot
In vitro synthesis of the iron-molybdenum cofactor of nitrogenase. Purification and characterization of NifB cofactor, the product of NIFB protein.
inferredcites →https://doi.org/10.1016/s0021-9258(18)66867-xopenalex-snapshot
Isolation and characterization of a second nitrogenase Fe-protein from Azotobacter vinelandii.
inferredcites →https://doi.org/10.1016/s0021-9258(19)88656-8openalex-snapshot
Nitrogenase-catalyzed ethane production and CO-sensitive hydrogen evolution from MoFe proteins having amino acid substitutions in an alpha-subunit FeMo cofactor-binding domain.
inferredcites →https://doi.org/10.1021/bi00009a008openalex-snapshot
Role of the MoFe Protein .alpha.-Subunit Histidine-195 Residue in FeMo-cofactor Binding and Nitrogenase Catalysis
inferredcites →https://doi.org/10.1021/bi00009a009openalex-snapshot
Electron Spin Echo Envelope Modulation Spectroscopic Analysis of Altered Nitrogenase MoFe Proteins from Azotobacter vinelandii
inferredcites →https://doi.org/10.1021/bi00371a001openalex-snapshot
Isolation of a new vanadium-containing nitrogenase from Azotobacter vinelandii
inferredcites →https://doi.org/10.1021/bi00381a001openalex-snapshot
Characterization of the metal clusters in the nitrogenase molybdenum-iron and vanadium-iron proteins of Azotobacter vinelandii using magnetic circular dichroism spectroscopy
inferredcites →https://doi.org/10.1021/bi00466a014openalex-snapshot
Apodinitrogenase: purification, association with a 20-kilodalton protein, and activation by the iron-molybdenum cofactor in the absence of dinitrogenase reductase
inferredcites →https://doi.org/10.1021/bi951429jopenalex-snapshot
Isolation of Two Forms of the Nitrogenase VFe Protein from Azotobacter vinelandii
inferredcites →https://doi.org/10.1021/bi951430iopenalex-snapshot
Oxidative Titration of the Nitrogenase VFe Protein from Azotobacter vinelandii: An Example of Redox-Gated Electron Flow
inferredcites →https://doi.org/10.1021/cr00106a002openalex-snapshot
The iron-molybdenum cofactor of nitrogenase
inferredcites →https://doi.org/10.1021/ja00048a034openalex-snapshot
Moessbauer and integer-spin EPR of the oxidized P-clusters of nitrogenase: POX is a non-Kramers system with a nearly degenerate ground doublet
inferredcites →https://doi.org/10.1021/ja00066a019openalex-snapshot
Iron EXAFS of Azotobacter vinelandii nitrogenase molybdenum-iron and vanadium-iron proteins
inferredcites →https://doi.org/10.1021/ja00074a050openalex-snapshot
Detection of EPR signals assigned to the 1-equiv-oxidized P-clusters of the nitrogenase MoFe-protein from Azotobacter vinelandii
inferredcites →https://doi.org/10.1021/ja00105a080openalex-snapshot
Construction and Characterization of Hybrid Component 1 from V-Nitrogenase Containing FeMo Cofactor
inferredcites →https://doi.org/10.1021/ja00138a033openalex-snapshot
Investigation of CO bound to inhibited forms of nitrogenase MoFe protein by 13C ENDOR
inferredcites →https://doi.org/10.1021/ja00204a035openalex-snapshot
Detection of a new signal in the ESR spectrum of vanadium nitrogenase from Azotobacter vinelandii
inferredcites →https://doi.org/10.1021/ja00220a066openalex-snapshot
X-ray absorption of Azotobacter vinelandii vanadium nitrogenase
inferredcites →https://doi.org/10.1021/ja953124yopenalex-snapshot
Unusual Effect of CO on C2H2 Reduction by V Nitrogenase from Azotobacter vinelandii
inferredcites →https://doi.org/10.1038/322388a0openalex-snapshot
The alternative nitrogenase of Azotobacter chroococcum is a vanadium enzyme
inferredcites →https://doi.org/10.1038/325372a0openalex-snapshot
Vanadium K-edge X-ray absorption spectrum of the VFe protein of the vanadium nitrogenase of Azotobacter chroococcum
inferredcites →https://doi.org/10.1038/327167a0openalex-snapshot
Ethane formation from acetylene as a potential test for vanadium nitrogenase in vivo
inferredcites →https://doi.org/10.1038/343188a0openalex-snapshot
Role for the nitrogenase MoFe protein α-subunit in FeMo-cofactor binding and catalysis
inferredcites →https://doi.org/10.1039/dt9940002739openalex-snapshot
Dalton perspectives. Metals in the nitrogenases
inferredcites →https://doi.org/10.1042/bj1250449openalex-snapshot
Microbial oxidation of amines. Partial purification of a mixed-function secondary-amine oxidase system from Pseudomonas aminovorans that contains an enzymically active cytochrome- P -420-type haemoprotein
inferredcites →https://doi.org/10.1042/bj2170317openalex-snapshot
Nitrogenase from nifV mutants of Klebsiella pneumoniae contains an altered form of the iron-molybdenum cofactor
inferredcites →https://doi.org/10.1042/bj2380437openalex-snapshot
Nitrogen fixation in molybdenum-deficient continuous culture by a strain of Azotobacter vinelandii carrying a deletion of the structural genes for nitrogenase (nifHDK)
inferredcites →https://doi.org/10.1042/bj2440197openalex-snapshot
The vanadium nitrogenase of Azotobacter chroococcum. Purification and properties of the VFe protein
inferredcites →https://doi.org/10.1042/bj2490745openalex-snapshot
The vanadium nitrogenase of Azotobacter chroococcum. Reduction of acetylene and ethylene to ethane
inferredcites →https://doi.org/10.1042/bj2500299openalex-snapshot
The vanadium-iron protein of vanadium nitrogenase from Azotobacter chroococcum contains an iron-vanadium cofactor
inferredcites →https://doi.org/10.1042/bj2510165openalex-snapshot
The vanadium- and molybdenum-containing nitrogenases of Azotobacter chroococcum. Comparison of mid-point potentials and kinetics of reduction by sodium dithionite of the iron proteins with bound magnesium adenosine 5′-diphosphate
inferredcites →https://doi.org/10.1042/bj2560429openalex-snapshot
Molybdenum and vanadium nitrogenases of Azotobacter chroococcum. Low temperature favours N2 reduction by vanadium nitrogenase
inferredcites →https://doi.org/10.1042/bj2570789openalex-snapshot
Vanadium nitrogenase of Azotobacter chroococcum. MgATP-dependent electron transfer within the protein complex
inferredcites →https://doi.org/10.1042/bj2580733openalex-snapshot
Vanadium K -edge X-ray-absorption spectroscopy of the functioning and thionine-oxidized forms of the VFe-protein of the vanadium nitrogenase from Azotobacter chroococcum
inferredcites →https://doi.org/10.1042/bj2770465openalex-snapshot
Hydrazine is a product of dinitrogen reduction by the vanadium-nitrogenase from Azotobacter chroococcum
inferredcites →https://doi.org/10.1042/bj2890395openalex-snapshot
The molybdenum and vanadium nitrogenases of Azotobacter chroococcum: effect of elevated temperature on N2 reduction
inferredcites →https://doi.org/10.1042/bj2920093openalex-snapshot
Klebsiella pneumoniae nitrogenase: pre-steady-state absorbance changes show that redox changes occur in the MoFe protein that depend on substrate and component protein ratio; a role for P-centres in reducing dinitrogen?
inferredcites →https://doi.org/10.1042/bj2930101openalex-snapshot
Molybdenum-independent nitrogenases of Azotobacter vinelandii: a functional species of alternative nitrogenase-3 isolated from a molybdenum-tolerant strain contains an iron-molybdenum cofactor
inferredcites →https://doi.org/10.1073/pnas.74.8.3249openalex-snapshot
Isolation of an iron-molybdenum cofactor from nitrogenase
inferredcites →https://doi.org/10.1073/pnas.77.12.7342openalex-snapshot
Evidence for an alternative nitrogen fixation system in Azotobacter vinelandii.
inferredcites →https://doi.org/10.1073/pnas.88.15.6620openalex-snapshot
N coordination of FeMo cofactor requires His-195 of the MoFe protein alpha subunit and is essential for biological nitrogen fixation.
inferredcites →https://doi.org/10.1073/pnas.90.7.2754openalex-snapshot
Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis.
inferredcites →https://doi.org/10.1074/jbc.270.42.24745openalex-snapshot
Characterization of the γ Protein and Its Involvement in the Metallocluster Assembly and Maturation of Dinitrogenase from Azotobacter vinelandii
inferredcites →https://doi.org/10.1074/jbc.270.45.26890openalex-snapshot
Incorporation of Iron and Sulfur from NifB Cofactor into the Iron-Molybdenum Cofactor of Dinitrogenase
inferredcites →https://doi.org/10.1074/jbc.270.45.27007openalex-snapshot
Involvement of the P Cluster in Intramolecular Electron Transfer within the Nitrogenase MoFe Protein
inferredcites →https://doi.org/10.1074/jbc.270.9.4432openalex-snapshot
Characteristics of NIFNE in Azotobacter vinelandii Strains
inferredcites →https://doi.org/10.1099/00221287-134-4-931openalex-snapshot
Further Analysis of Nitrogen Fixation (nif) Genes in Azotobacter chroococcum: Identification and Expression in Klebsiella pneumoniae of nifS, nifV, nifM and nifB Genes and Localization of nifE/N-, nifU-, nifA- and fix ABC-like Genes
inferredcites →https://doi.org/10.1111/j.1365-2958.1990.tb02060.xopenalex-snapshot
Analysis of site‐directed mutations in the α‐and β‐subunits of Klebsiella pneumoniae nitrogenase
inferredcites →https://doi.org/10.1111/j.1365-2958.1993.tb01611.xopenalex-snapshot
Characterization of anf genes specific for the alternative nitrogenase and identification of nif genes required for both nitrogenases in Rhodobacter capsulatus
inferredcites →https://doi.org/10.1111/j.1432-1033.1987.tb13633.xopenalex-snapshot
Quantitative EPR of an S = 7/2 system in thionine‐oxidized MoFe proteins of nitrogenase
inferredcites →https://doi.org/10.1111/j.1432-1033.1991.tb15750.xopenalex-snapshot
Demonstration of a molybdenum‐ and vanadium‐independent nitrogenase in a nifHDK‐deletion mutant of Rhodobacter capsulatus
inferredcites →https://doi.org/10.1111/j.1432-1033.1992.tb16746.xopenalex-snapshot
Metalloclusters of the nitrogenases
inferredcites →https://doi.org/10.1111/j.1432-1033.1993.tb17632.xopenalex-snapshot
Redox properties and EPR spectroscopy of the P clusters of Azotobacter vinelandii MoFe protein
inferredcites →https://doi.org/10.1111/j.1432-1033.1993.tb18003.xopenalex-snapshot
Detection of the in vivo incorporation of a metal cluster into a protein
inferredcites →https://doi.org/10.1111/j.1432-1033.1995.0014l.xopenalex-snapshot
The Mechanism of Dinitrogen Reduction by Molybdenum Nitrogenases
inferredcites →https://doi.org/10.1111/j.1432-1033.1995.0666h.xopenalex-snapshot
The Molybdenum Nitrogenase from Wild-type Xanthobacter autotrophicus Exhibits Properties Reminiscent of Alternative Nitrogenases
inferredcites →https://doi.org/10.1111/j.1574-6968.1988.tb02960.xopenalex-snapshot
Evidence for the occurrence of the alternative, vanadium-containing nitrogenase in the cyanobacteriumAnabaena variabilis
inferredcites →https://doi.org/10.1126/science.1529354openalex-snapshot
Structural Models for the Metal Centers in the Nitrogenase Molybdenum-Iron Protein
inferredcites →https://doi.org/10.1126/science.232.4746.92openalex-snapshot
Nitrogen Fixation by Azotobacter vinelandii Strains Having Deletions in Structural Genes for Nitrogenase
inferredcites →https://doi.org/10.1126/science.8484118openalex-snapshot
The Nitrogenase FeMo-Cofactor and P-Cluster pair: 2.2 Å Resolution Structures
inferredcites →https://doi.org/10.1128/aem.57.2.622-624.1991openalex-snapshot
Temperature-Dependent Regulation by Molybdenum and Vanadium of Expression of the Structural Genes Encoding Three Nitrogenases in Azotobacter vinelandii
inferredcites →https://doi.org/10.1128/jb.170.1.27-33.1988openalex-snapshot
Purification of a second alternative nitrogenase from a nifHDK deletion strain of Azotobacter vinelandii
inferredcites →https://doi.org/10.1128/jb.171.1.124-129.1989openalex-snapshot
Genetic evidence for an Azotobacter vinelandii nitrogenase lacking molybdenum and vanadium
inferredcites →https://doi.org/10.1128/jb.171.2.1017-1027.1989openalex-snapshot
Physical and genetic map of the major nif gene cluster from Azotobacter vinelandii
inferredcites →https://doi.org/10.1128/jb.171.2.1075-1086.1989openalex-snapshot
Nucleotide sequence and mutational analysis of the structural genes (anfHDGK) for the second alternative nitrogenase from Azotobacter vinelandii
inferredcites →https://doi.org/10.1128/jb.172.6.3400-3408.1990openalex-snapshot
Nucleotide sequences and mutational analysis of the structural genes for nitrogenase 2 of Azotobacter vinelandii
inferredcites →https://doi.org/10.1128/jb.173.17.5457-5469.1991openalex-snapshot
Nucleotide sequence and genetic analysis of the Azotobacter chroococcum nifUSVWZM gene cluster, including a new gene (nifP) which encodes a serine acetyltransferase
inferredcites →https://doi.org/10.1128/jb.173.18.5705-5711.1991openalex-snapshot
Identification of an alternative nitrogenase system in Rhodospirillum rubrum
inferredcites →https://doi.org/10.1128/jb.173.23.7565-7572.1991openalex-snapshot
Nucleotide sequence and mutational analysis of the vnfENX region of Azotobacter vinelandii
inferredcites →https://doi.org/10.1128/jb.175.15.4907-4910.1993openalex-snapshot
The nifY product of Klebsiella pneumoniae is associated with apodinitrogenase and dissociates upon activation with the iron-molybdenum cofactor
inferredcites →https://doi.org/10.1128/jb.175.19.6276-6286.1993openalex-snapshot
Characterization of genes for an alternative nitrogenase in the cyanobacterium Anabaena variabilis
inferredcites →https://doi.org/10.1128/jb.175.21.6737-6744.1993openalex-snapshot
Nitrogenase metalloclusters: structures, organization, and synthesis
inferredcites →https://doi.org/10.1128/jb.177.6.1505-1510.1995openalex-snapshot
The genes encoding the delta subunits of dinitrogenases 2 and 3 are required for mo-independent diazotrophic growth by Azotobacter vinelandii
inferredcites →https://doi.org/10.1128/jb.177.6.1570-1575.1995openalex-snapshot
Characterization of nifB, nifS, and nifU genes in the cyanobacterium Anabaena variabilis: NifB is required for the vanadium-dependent nitrogenase
inferredcites →https://doi.org/10.1128/jb.178.1.204-208.1996openalex-snapshot
Characteristics of orf1 and orf2 in the anfHDGK genomic region encoding nitrogenase 3 of Azotobacter vinelandii
inferredcites →https://doi.org/10.1139/m89-053openalex-snapshot
A comparison of the three dinitrogenase reductases expressed by Azotobacter vinelandii
inferredcites →https://doi.org/10.1201/9781482293074openalex-snapshot
Metal Ions in Biological Systems
inferredcites →https://doi.org/10.3109/10408418809104465openalex-snapshot
Bacterial Alternative Nitrogen Fixation Systems

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4772837openalex-extracted
Comparison of Protonation and Anion Binding Preference of Chatt-Type Tungsten Dinitrogen Complex: Dft Studies
inferred← citeshttps://doi.org/10.1002/(sici)1097-461x(1998)70:6<1159::aid-qua5>3.0.co;2-zopenalex-snapshot
Studies on the hydrogenation steps of the nitrogen molecule at theAzotobacter vinelandii nitrogenase site
inferred← citeshttps://doi.org/10.1002/(sici)1099-0682(200005)2000:5<1079::aid-ejic1079>3.0.co;2-vopenalex-snapshot
Coordination of CO, NO, N2H2, and Other Nitrogenase Relevant Small Molecules to Sulfur-Rich Ruthenium Complexes with the New Ligand ‘tpS4’2– = 1,2-Bis(2-mercaptophenylthio)phenylene(2–)
inferred← citeshttps://doi.org/10.1002/(sici)1521-3757(19981002)110:19<2780::aid-ange2780>3.0.co;2-gopenalex-snapshot
Neue Entwicklungen in der Stickstoff-Fixierung
inferred← citeshttps://doi.org/10.1002/(sici)1521-3757(19990712)111:13/14<2142::aid-ange2142>3.0.co;2-copenalex-snapshot
Modellierung einer Nitrogenase-Schlüsselreaktion: die N2-abhängige HD-Bildung durch D2/H+-Austausch
inferred← citeshttps://doi.org/10.1002/(sici)1521-3757(19991216)111:24<3890::aid-ange3890>3.0.co;2-kopenalex-snapshot
Stickstoffixierung: Reduktion von N2 durch vier Metallfragmente unter Bildung eines vierkernigen Samarium-Distickstoffkomplexes
inferred← citeshttps://doi.org/10.1002/0470028637.met174openalex-snapshot
Nitrogenase
inferred← citeshttps://doi.org/10.1002/0470862106.ia158openalex-snapshot
Nitrogenase: Metal Cluster Models
inferred← citeshttps://doi.org/10.1002/0470862106.ia159openalex-snapshot
Nitrogenase Catalysis & AssemblyBased in part on the article Nitrogenases & the Iron–Molybdenum Cofactor by Paul W. Ludden which appeared in theEncyclopedia of Inorganic Chemistry, First Edition.
inferred← citeshttps://doi.org/10.1002/0470862106.ia253openalex-snapshot
Vanadium: Inorganic & Coordination ChemistryBased in part on the article Vanadium: Inorganic & Coordination Chemistry by Elizabeth M. Page & Sherilyn A. Wass which appeared in the Encyclopedia of Inorganic Chemistry, First Edition .
inferred← citeshttps://doi.org/10.1002/0470862106.ia272openalex-snapshot
Metal‐Based Drugs
inferred← citeshttps://doi.org/10.1002/047120918x.emb1004openalex-snapshot
Nitrogen Fixation
inferred← citeshttps://doi.org/10.1002/0471227617.eoc017openalex-snapshot
Ammonia Synthesis – Biological
inferred← citeshttps://doi.org/10.1002/0471227617.eoc017.pub2openalex-snapshot
Ammonia Synthesis—Biological
inferred← citeshttps://doi.org/10.1002/0471227617.eoc153openalex-snapshot
Multimetallic Catalysts – Homogeneous
inferred← citeshttps://doi.org/10.1002/0471238961.1409201814052320.a01.pub2openalex-snapshot
Nitrogen Fixation
inferred← citeshttps://doi.org/10.1002/0471238961.1409201814052320.a01.pub3openalex-snapshot
Nitrogen Fixation
inferred← citeshttps://doi.org/10.1002/1099-0682(200104)2001:4<935::aid-ejic935>3.0.co;2-jopenalex-snapshot
Vanadium(IV and V) Complexes ContainingSNO (Dithiocarbonylhydrazone; Thiosemicarbazone) Donor Sets
inferred← citeshttps://doi.org/10.1002/1099-0682(200106)2001:6<1441::aid-ejic1441>3.0.co;2-gopenalex-snapshot
On the Relevance of Mono- and Dinuclear Iron Carbonyl Complexes to the Fixation and Stepwise Hydrogenation of N2
inferred← citeshttps://doi.org/10.1002/14356007.a17_471.pub2openalex-snapshot
Nitrogen Fixation
inferred← citeshttps://doi.org/10.1002/1521-3765(20010504)7:9<1874::aid-chem1874>3.0.co;2-2openalex-snapshot
Synthesis, Reactivity, and Structure of Strictly Homologous 18 and 19 Valence Electron Iron Nitrosyl Complexes
inferred← citeshttps://doi.org/10.1002/1521-3765(20011203)7:23<5195::aid-chem5195>3.0.co;2-3openalex-snapshot
Dinuclear Diazene Iron and Ruthenium Complexes as Models for Studying Nitrogenase Activity
inferred← citeshttps://doi.org/10.1002/9780470048672.wecb706openalex-snapshot
Iron–Sulfur Clusters: Properties and Functions
inferred← citeshttps://doi.org/10.1002/9780470166512.ch6openalex-snapshot
The Chemistry of Synthetic Fe–Mo–S Clusters and their Relevance to the Structure and Function of the Fe–Mo–S Center in Nitrogenase
inferred← citeshttps://doi.org/10.1002/9780470281840.ch13openalex-snapshot
Molecular Ecological Aspects of Nitrogen Fixation in the Marine Environment
inferred← citeshttps://doi.org/10.1002/9781118357514.biblioopenalex-snapshot
Bibliography
inferred← citeshttps://doi.org/10.1002/9781118802236.ch05openalex-snapshot
Iron Proteins
inferred← citeshttps://doi.org/10.1002/9781119053095.ch109openalex-snapshot
Environmental and Economic Impacts of Biological Nitrogen‐Fixing (BNF) Cereal Crops
inferred← citeshttps://doi.org/10.1002/9781119053095.ch16openalex-snapshot
Exploring Alternative Paths for the Evolution of Biological Nitrogen Fixation
inferred← citeshttps://doi.org/10.1002/9781119053095.ch2openalex-snapshot
Recent Advances in Understanding Nitrogenases and How They Work
inferred← citeshttps://doi.org/10.1002/9781119053095.ch8openalex-snapshot
Distribution and Ecological Niches of Nitrogenases
inferred← citeshttps://doi.org/10.1002/9781119053095.ch9openalex-snapshot
Regulation of nif Gene Expression in Azotobacter vinelandii
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0148openalex-snapshot
Nitrogenase: Metal Cluster Models
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0148.pub2openalex-snapshot
Nitrogenase: Metal Cluster Models
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0149openalex-snapshot
Nitrogenase Catalysis & AssemblyBased in part on the article Nitrogenases & the Iron–Molybdenum Cofactor by Paul W. Ludden which appeared in theEncyclopedia of Inorganic Chemistry, First Edition.
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0149.pub2openalex-snapshot
Nitrogenase Assembly and CatalysisUpdate based on the original article by Yilin Hu, Benedikt Schmid & Markus W. Ribbe,Encyclopedia of Inorganic ChemistrySecond Edition, © 2005, John Wiley & Sons, Ltd
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0236openalex-snapshot
Vanadium: Inorganic & Coordination ChemistryBased in part on the article Vanadium: Inorganic & Coordination Chemistry by Elizabeth M. Page & Sherilyn A. Wass which appeared in the Encyclopedia of Inorganic Chemistry, First Edition .
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0254openalex-snapshot
Metal‐Based Drugs
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0601openalex-snapshot
Nitrogenase
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc2466openalex-snapshot
FeS Cluster Assembly: NIF System in Nitrogen‐Fixing Bacteria
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc2471openalex-snapshot
Assembly of Nitrogenase FeMoco and P Cluster
inferred← citeshttps://doi.org/10.1002/9781119986782.ch8openalex-snapshot
Environmental Variability and Its Control of Productivity
inferred← citeshttps://doi.org/10.1002/9783527618248.ch29openalex-snapshot
Electron Transfer in Catalytic Dinitrogen Reduction
inferred← citeshttps://doi.org/10.1002/9783527631582.ch2openalex-snapshot
Catalytic Reduction of Dinitrogen to Ammonia by Molybdenum
inferred← citeshttps://doi.org/10.1002/9783527664160.ch10openalex-snapshot
A Unified Chemical Mechanism for Hydrogenation Reactions Catalyzed by Nitrogenase
inferred← citeshttps://doi.org/10.1002/9783527664160.ch8openalex-snapshot
Structures and Functions of the Active Sites of Nitrogenases
inferred← citeshttps://doi.org/10.1002/9783527843596.ch10openalex-snapshot
Alternative Substrates of Nitrogenase
inferred← citeshttps://doi.org/10.1002/9783527846368.ch19openalex-snapshot
Metal‐Based Nanomaterials for Electrocatalytic Nitrogen Reduction Reaction
inferred← citeshttps://doi.org/10.1002/adfm.202002731openalex-snapshot
Photoelectrochemical Synthesis of Ammonia with Black Phosphorus
inferred← citeshttps://doi.org/10.1002/advs.202103583openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/aenm.201800369openalex-snapshot
A Review of Electrocatalytic Reduction of Dinitrogen to Ammonia under Ambient Conditions
inferred← citeshttps://doi.org/10.1002/aenm.201801357openalex-snapshot
Boosted Electrocatalytic N 2 Reduction to NH 3 by Defect‐Rich MoS 2 Nanoflower
inferred← citeshttps://doi.org/10.1002/aenm.201902020openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/aenm.202501867openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/ange.200390273openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/ange.200460415openalex-snapshot
Diazene Complexes of Copper: Synthesis, Spectroscopic Analysis, and Electronic Structure
inferred← citeshttps://doi.org/10.1002/ange.200502892openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/ange.200705246openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/ange.200801668openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/ange.201100869openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/ange.201102979openalex-snapshot
Fischer‐Tropsch‐Chemie bei Raumtemperatur?
inferred← citeshttps://doi.org/10.1002/ange.201108916openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/ange.201406863openalex-snapshot
Differential Reduction of CO2 by Molybdenum and Vanadium Nitrogenases
inferred← citeshttps://doi.org/10.1002/ange.201408725openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/ange.201410412openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/ange.201507646openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/ange.201600010openalex-snapshot
Nitrogenase – eine Geschichte von Kohlenstoffatomen
inferred← citeshttps://doi.org/10.1002/ange.201901899openalex-snapshot
X‐ray Magnetic Circular Dichroism Spectroscopy Applied to Nitrogenase and Related Models: Experimental Evidence for a Spin‐Coupled Molybdenum(III) Center
inferred← citeshttps://doi.org/10.1002/ange.202012357openalex-snapshot
Graphdiyne@Janus Magnetite for Photocatalytic Nitrogen Fixation
inferred← citeshttps://doi.org/10.1002/ange.202015751openalex-snapshot
Structural Characterization of Two CO Molecules Bound to the Nitrogenase Active Site
inferred← citeshttps://doi.org/10.1002/ange.202208544openalex-snapshot
Proton Transfer Pathways in Nitrogenase with and without Dissociated S2B
inferred← citeshttps://doi.org/10.1002/ange.8683437openalex-snapshot
Gain‐of‐Function Engineering of the NifEN Scaffold Into a Self‐Assembling Nitrogenase
inferred← citeshttps://doi.org/10.1002/anie.200390302openalex-snapshot
The Role of Mo Atoms in Nitrogen Fixation: Balancing Substrate Reduction and Dihydrogen Production
inferred← citeshttps://doi.org/10.1002/anie.200460415openalex-snapshot
Diazene Complexes of Copper: Synthesis, Spectroscopic Analysis, and Electronic Structure
inferred← citeshttps://doi.org/10.1002/anie.200502892openalex-snapshot
Intrinsic Dinitrogen Activation at Bare Metal Atoms
inferred← citeshttps://doi.org/10.1002/anie.200705246openalex-snapshot
Catalytic Reduction of Dinitrogen to Ammonia by Molybdenum: Theory versus Experiment
inferred← citeshttps://doi.org/10.1002/anie.200801668openalex-snapshot
Energetics and Mechanism of Dinitrogen Cleavage at a Mononuclear Surface Tantalum Center: A New Way of Dinitrogen Reduction
inferred← citeshttps://doi.org/10.1002/anie.201100869openalex-snapshot
Tracing the Hydrogen Source of Hydrocarbons Formed by Vanadium Nitrogenase
inferred← citeshttps://doi.org/10.1002/anie.201102979openalex-snapshot
Fischer–Tropsch Chemistry at Room Temperature?
inferred← citeshttps://doi.org/10.1002/anie.201108916openalex-snapshot
ATP‐Independent Formation of Hydrocarbons Catalyzed by Isolated Nitrogenase Cofactors
inferred← citeshttps://doi.org/10.1002/anie.201406863openalex-snapshot
Differential Reduction of CO2 by Molybdenum and Vanadium Nitrogenases
inferred← citeshttps://doi.org/10.1002/anie.201408725openalex-snapshot
Synthesis and Ligand Modification Chemistry of a Molybdenum Dinitrogen Complex: Redox and Chemical Activity of a Bis(imino)pyridine Ligand
inferred← citeshttps://doi.org/10.1002/anie.201410412openalex-snapshot
Catalytic Reduction of CN−, CO, and CO2 by Nitrogenase Cofactors in Lanthanide‐Driven Reactions
inferred← citeshttps://doi.org/10.1002/anie.201507646openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/anie.201600010openalex-snapshot
Nitrogenases—A Tale of Carbon Atom(s)
inferred← citeshttps://doi.org/10.1002/anie.201901899openalex-snapshot
X‐ray Magnetic Circular Dichroism Spectroscopy Applied to Nitrogenase and Related Models: Experimental Evidence for a Spin‐Coupled Molybdenum(III) Center
inferred← citeshttps://doi.org/10.1002/anie.202012357openalex-snapshot
Graphdiyne@Janus Magnetite for Photocatalytic Nitrogen Fixation
inferred← citeshttps://doi.org/10.1002/anie.202015751openalex-snapshot
Structural Characterization of Two CO Molecules Bound to the Nitrogenase Active Site
inferred← citeshttps://doi.org/10.1002/anie.202208544openalex-snapshot
Proton Transfer Pathways in Nitrogenase with and without Dissociated S2B
inferred← citeshttps://doi.org/10.1002/anie.8683437openalex-snapshot
Gain‐of‐Function Engineering of the NifEN Scaffold Into a Self‐Assembling Nitrogenase
inferred← citeshttps://doi.org/10.1002/aoc.1327openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/aoc.6644openalex-snapshot
Molybdenum bound nitrogen‐doped graphene catalyst for reduction of N2 to NH3 and NH2NH2, using FLP as a co‐catalyst: A DFT study
inferred← citeshttps://doi.org/10.1002/aoc.7001openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/aoc.7067openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/aoc.744openalex-snapshot
Why do nitrogenases waste electrons by evolving dihydrogen?
inferred← citeshttps://doi.org/10.1002/asia.201700478openalex-snapshot
Nitrogenase Cofactor: Inspiration for Model Chemistry
inferred← citeshttps://doi.org/10.1002/asia.201700624openalex-snapshot
Activation of CO2 by Vanadium Nitrogenase
inferred← citeshttps://doi.org/10.1002/asia.202500657openalex-snapshot
An Overview on Transition Metal Catalyzed Ammonia Generation Through N─N Bond Cleavage of Hydrazine
inferred← citeshttps://doi.org/10.1002/bit.26076openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/btpr.406openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/cbdv.200890136openalex-snapshot
Vanadium Detoxification: Chemical and Biochemical Aspects
inferred← citeshttps://doi.org/10.1002/cbic.201500305openalex-snapshot
Widening the Product Profile of Carbon Dioxide Reduction by Vanadium Nitrogenase
inferred← citeshttps://doi.org/10.1002/cbic.201800035openalex-snapshot
A Comparative Analysis of the CO‐Reducing Activities of MoFe Proteins Containing Mo‐ and V‐Nitrogenase Cofactors
inferred← citeshttps://doi.org/10.1002/cbic.201900654openalex-snapshot
A V‐Nitrogenase Variant Containing a Citrate‐Substituted Cofactor
inferred← citeshttps://doi.org/10.1002/cbic.201900782openalex-snapshot
Divergent Members of the Nitrogenase Superfamily: Tetrapyrrole Biosynthesis and Beyond
inferred← citeshttps://doi.org/10.1002/cbic.201900785openalex-snapshot
Chlorophyllide a oxidoreductase Preferentially Catalyzes 8‐Vinyl Reduction over B‐Ring Reduction of 8‐Vinyl Chlorophyllide a in the Late Steps of Bacteriochlorophyll Biosynthesis
inferred← citeshttps://doi.org/10.1002/cbic.202000022openalex-snapshot
Distribution of Nitrogen‐Fixation Genes in Prokaryotes Containing Alternative Nitrogenases
inferred← citeshttps://doi.org/10.1002/cbic.202100453openalex-snapshot
The Conversion of Carbon Monoxide and Carbon Dioxide by Nitrogenases
inferred← citeshttps://doi.org/10.1002/cbic.202500366openalex-snapshot
Reductant‐ or Light‐Driven ATP‐Independent Reduction of CO2 by Nitrogenase MoFe Protein
inferred← citeshttps://doi.org/10.1002/cbic.202500541openalex-snapshot
Deserts, Rivers, Pools, and Billabongs: Water Features of the Nitrogenase Proteins, and their Functions
inferred← citeshttps://doi.org/10.1002/cctc.201200635openalex-snapshot
First‐Principles Calculations of Fischer–Tropsch Processes Catalyzed by Nitrogenase Enzymes
inferred← citeshttps://doi.org/10.1002/ceat.202000527openalex-snapshot
Biohydrogen Machinery: Recent Insights, Genetic Fabrication, and Future Prospects
inferred← citeshttps://doi.org/10.1002/celc.201801484openalex-snapshot
Electrocatalytic N2 Fixation over Hollow VO2 Microspheres at Ambient Conditions
inferred← citeshttps://doi.org/10.1002/celc.202200625openalex-snapshot
In‐Situ‐Generated MoO2 on MoS2/ZnO Heterostructures with Enriched S,O‐Vacancies for Enhanced Electrocatalytic Reduction of N2 to NH3
inferred← citeshttps://doi.org/10.1002/chem.200204627openalex-snapshot
Synthesis and Characterization of New Five‐Coordinate Platinum Nitrosyl Derivatives: Density Functional Theory Study of Their Electronic Structure
inferred← citeshttps://doi.org/10.1002/chem.200400081openalex-snapshot
A Photochemical Activation Scheme of Inert Dinitrogen by Dinuclear RuII and FeII Complexes
inferred← citeshttps://doi.org/10.1002/chem.200400580openalex-snapshot
An Electronic Perspective on the Reduction of an NN Double Bond at a Conserved Dimolybdenum Core
inferred← citeshttps://doi.org/10.1002/chem.201702496openalex-snapshot
Synthetic Analogues of Nitrogenase Metallocofactors: Challenges and Developments
inferred← citeshttps://doi.org/10.1002/chem.201704378openalex-snapshot
Tuning Electron Flux through Nitrogenase with Methanogen Iron Protein Homologues
inferred← citeshttps://doi.org/10.1002/chem.201803735openalex-snapshot
Strategies Towards Capturing Nitrogenase Substrates and Intermediates via Controlled Alteration of Electron Fluxes
inferred← citeshttps://doi.org/10.1002/chem.202103933openalex-snapshot
Thermodynamically Favourable States in the Reaction of Nitrogenase without Dissociation of any Sulfide Ligand
inferred← citeshttps://doi.org/10.1002/chin.199710280openalex-snapshot
ChemInform Abstract: Structure‐Function Relationships of Alternative Nitrogenases
inferred← citeshttps://doi.org/10.1002/cnma.202000110openalex-snapshot
Greatly Enhanced Electrocatalytic N2 Reduction over V2O3/C by P Doping
inferred← citeshttps://doi.org/10.1002/cphc.200400474openalex-snapshot
Towards an Understanding of the Workings of Nitrogenase from DFT Calculations
inferred← citeshttps://doi.org/10.1002/cplu.202500184openalex-snapshot
Catalysts for Ammonia Electrosynthesis by Nitrogen Reduction: Recent Progress
inferred← citeshttps://doi.org/10.1002/cssc.70788openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/ecy.3211openalex-snapshot
Molybdenum, phosphorus, and pH do not constrain nitrogen fixation in a tropical forest in the southeastern Amazon
inferred← citeshttps://doi.org/10.1002/ejic.200300519openalex-snapshot
New Pentadentate Carboxylate‐Derivatized Sulfur Ligands Affording Water Soluble Iron Complexes with [Fe(NS4)] Cores that Bind Small Molecules (CO, NO, PMe3) as Co‐Ligands
inferred← citeshttps://doi.org/10.1002/ejic.200390058openalex-snapshot
Synthesis, Structure and Reactivity of Sulfur‐Rich [Fe(L1)(L2)(‘tpS4’)] Complexes with Rigid [Fe(‘tpS4’] Cores and σ−π Co‐Ligands (‘tpS4’2− = 1,2‐Bis(2‐mercaptophenylthio)phenylene(2−); L1, L2 = CO, PR3, NO)
inferred← citeshttps://doi.org/10.1002/ejic.200390119openalex-snapshot
A Dinuclear Iron Complex with Two Cofacial [FeS4] Cores Linked by Covalent Ligand Periphery Clamps and Dissociable Thiolate Bridges
inferred← citeshttps://doi.org/10.1002/ejic.200400066openalex-snapshot
Ruthenium( II ) and Ruthenium( III ) Complexes Containing the [pyS4]2− Ligand [pyS42− = 2,6‐Bis(2‐mercaptophenylthio)dimethylpyridine(2−)]
inferred← citeshttps://doi.org/10.1002/ejic.200400375openalex-snapshot
Reactivity of a Thiolate‐Bridged Dinuclear Ruthenium Complex with Nitrogenous Molecules: Spectroscopic Identification of a Labile Dinitrogen Complex
inferred← citeshttps://doi.org/10.1002/ejic.200700143openalex-snapshot
Synthesis and Spectro‐electrochemical Aspects of [RuII(trpy)(pdt)(X)]n+ (trpy = 2,2′:6′,2″‐Terpyridine, pdt = 5,6‐Diphenyl‐3‐pyridyl‐as‐triazine, X = Cl–, CH3CN, NO2–, NO+, NO·) – Electrophilicity of {RuII–NO+} and Photolability of {RuII–NO·}
inferred← citeshttps://doi.org/10.1002/ejic.200900807openalex-snapshot
Mechanistic Information on the Reversible Binding of NO to Mono‐ and Dinuclear FeII Complexes of a Biomimetic S4N Ligand
inferred← citeshttps://doi.org/10.1002/ejic.201100218openalex-snapshot
Synthesis, Structure, and Behavior in Solution of the Dawson Thio Derivative [(P2W17O61)2(H4Mo4S4O6)]16–
inferred← citeshttps://doi.org/10.1002/ejic.201402080openalex-snapshot
Oxidative Addition of Rhodium Complexes Containing a Dithioimidodiphosphinate Ligand: Facile Reductive Elimination of Methyl Iodide from a Tetranuclear Rhodium Sulfido Cluster
inferred← citeshttps://doi.org/10.1002/ejic.201403041openalex-snapshot
Reactivity of Dinitrogen Bound to Mid‐ and Late‐Transition‐Metal Centers
inferred← citeshttps://doi.org/10.1002/ejic.201701326openalex-snapshot
Nitrogen Fixation Catalyzed by Transition Metal Complexes: Recent Developments
inferred← citeshttps://doi.org/10.1002/ejic.201800850openalex-snapshot
Syntheses, Structures and Reactivity of Terminal Phosphido Complexes of Iron(II) Supported by a β‐Diketiminato Ligand
inferred← citeshttps://doi.org/10.1002/ejic.201901120openalex-snapshot
Dinitrogen Activation by a Heterometallic VFe Complex Derived from 1,1'‐Bis(arylamido)vanadocene
inferred← citeshttps://doi.org/10.1002/ejic.202500016openalex-snapshot
Theoretical Study of Local Environmental Effect on Electronic Structure of M‐Cluster
inferred← citeshttps://doi.org/10.1002/ijch.201100009openalex-snapshot
A Decade of Oxothiomolybdenum Wheels: Synthesis, Behavior in Solution, and Electrocatalytic Properties
inferred← citeshttps://doi.org/10.1002/jobm.201100443openalex-snapshot
Investigating the effects of metals on phenol oxidase‐producing nitrogen‐fixing Azotobacter chroococcum
inferred← citeshttps://doi.org/10.1002/lol2.10220openalex-snapshot
Nitrogen fixation: A poorly understood process along the freshwater‐marine continuum
inferred← citeshttps://doi.org/10.1002/mbo3.265openalex-snapshot
Posttranslational modification of a vanadium nitrogenase
inferred← citeshttps://doi.org/10.1002/mbo3.921openalex-snapshot
NifA is the master regulator of both nitrogenase systems in Rhodobacter capsulatus
inferred← citeshttps://doi.org/10.1002/psc.538openalex-snapshot
Metal ion‐binding ability of tetrapeptides containing α‐aminoisobutyric acid
inferred← citeshttps://doi.org/10.1002/qua.10131openalex-snapshot
Semiempirical INDO/S calculations on the absorption spectrum of mono‐ and trinuclear vanadium(II) complexes
inferred← citeshttps://doi.org/10.1002/qua.20492openalex-snapshot
Enzymatic and catalytic reduction of dinitrogen to ammonia: Density functional theory characterization of alternative molybdenum active sites
inferred← citeshttps://doi.org/10.1002/qua.20987openalex-snapshot
Protonation of metal‐bound α‐hydroxycarboxylate ligand and implication for the role of homocitrate in nitrogenase: Computational study of the oxy‐bidentate chelate ring opening
inferred← citeshttps://doi.org/10.1002/qua.25627openalex-snapshot
Influence of the protein and DFT method on the broken‐symmetry and spin states in nitrogenase
inferred← citeshttps://doi.org/10.1002/slct.202204724openalex-snapshot
Pincer Ligand Supported Fe Complex Catalysed Dinitrogen Reduction to NH 3 Using FLP‐H 2 as the Hydrogen Source: DFT Studies
inferred← citeshttps://doi.org/10.1002/smtd.201800501openalex-snapshot
Nitrogen Reduction to Ammonia on Atomic‐Scale Active Sites under Mild Conditions
inferred← citeshttps://doi.org/10.1002/smtd.201900356openalex-snapshot
Greatly Enhanced Electrocatalytic N 2 Reduction on TiO 2 via V Doping
inferred← citeshttps://doi.org/10.1002/sstr.202200202openalex-snapshot
Recent Advances in Designing Efficient Electrocatalysts for Electrochemical Nitrate Reduction to Ammonia
inferred← citeshttps://doi.org/10.1002/sus2.13openalex-snapshot
Recent advances in TiO2‐based catalysts for N2 reduction reaction
inferred← citeshttps://doi.org/10.1002/zaac.201300081openalex-snapshot
New Synthetic Routes to Metal‐Sulfur Clusters Relevant to the Nitrogenase Metallo‐Clusters
inferred← citeshttps://doi.org/10.1002/zaac.201400114openalex-snapshot
N2 Binding to the FeMo‐Cofactor of Nitrogenase
inferred← citeshttps://doi.org/10.1002/zaac.201400378openalex-snapshot
Late Metal Scaffolds that Activate Both, Dinitrogen and Reduced Dinitrogen Species NxHy
inferred← citeshttps://doi.org/10.1006/bbrc.2002.6518openalex-snapshot
The Involvement of Molybdenum in Life
inferred← citeshttps://doi.org/10.1006/jmbi.1998.1898openalex-snapshot
Conformational variability in structures of the nitrogenase iron proteins from Azotobacter vinelandii and Clostridium pasteurianum
inferred← citeshttps://doi.org/10.1006/jmbi.1999.3107openalex-snapshot
New insights into structure-function relationships in nitrogenase: a 1.6 Å resolution X-ray crystallographic study of Klebsiella pneumoniae MoFe-protein
inferred← citeshttps://doi.org/10.1007/0-306-47597-9_10openalex-snapshot
Activation of Hydrogen and Related Small Molecules by Metalloenzymes and Sulfur Ligand Systems
inferred← citeshttps://doi.org/10.1007/0-306-47615-0_2openalex-snapshot
Chemistry and Biochemistry of Nitrogenase
inferred← citeshttps://doi.org/10.1007/0-306-47615-0_3openalex-snapshot
The Mechanism of Molybdenum Nitrogenase: An Overview
inferred← citeshttps://doi.org/10.1007/0-306-47615-0_8openalex-snapshot
Roles of VnfX and NifX in FeV-Co and FeMo-Co Synthesis in Azotobacter Vinelandii
inferred← citeshttps://doi.org/10.1007/0-387-30742-7_24openalex-snapshot
Dinitrogen-Fixing Prokaryotes
inferred← citeshttps://doi.org/10.1007/1-4020-4297-3_14openalex-snapshot
DIVERSITY, DISTRIBUTION AND BIOGEOCHEMICAL SIGNIFICANCE OF NITROGEN-FIXING MICROORGANISMS IN ANOXIC AND SUBOXIC OCEAN ENVIRONMENTS
inferred← citeshttps://doi.org/10.1007/3418_2016_4openalex-snapshot
Sulfur-Supported Iron Complexes for Understanding N2 Reduction
inferred← citeshttps://doi.org/10.1007/430_2018_26openalex-snapshot
Recent Advances in the Chemical Synthesis of Nitrogenase Model Clusters
inferred← citeshttps://doi.org/10.1007/978-1-0716-1605-5_6openalex-snapshot
Expression, Isolation, and Characterization of Vanadium Nitrogenase from Azotobacter vinelandii
inferred← citeshttps://doi.org/10.1007/978-1-4020-3611-8_10openalex-snapshot
Vanadium Nitrogenase
inferred← citeshttps://doi.org/10.1007/978-1-4020-3611-8_11openalex-snapshot
Iron-Only Nitrogenase: Exceptional Catalytic, Structural and Spectroscopic Features
inferred← citeshttps://doi.org/10.1007/978-1-4020-3611-8_5openalex-snapshot
The Mechanism of Mo-Dependent Nitrogenase: Thermodynamics and Kinetics
inferred← citeshttps://doi.org/10.1007/978-1-4614-1533-6_416openalex-snapshot
Indium, Physical and Chemical Properties
inferred← citeshttps://doi.org/10.1007/978-1-4615-4827-0_56openalex-snapshot
Nitrogen Fixation in the Marine Cyanobacterium Trichodesmium
inferred← citeshttps://doi.org/10.1007/978-1-4939-8864-8_1openalex-snapshot
Nitrogenases
inferred← citeshttps://doi.org/10.1007/978-1-4939-8864-8_6openalex-snapshot
Genomic Manipulations of the Diazotroph Azotobacter vinelandii
inferred← citeshttps://doi.org/10.1007/978-1-61779-194-9_17openalex-snapshot
Techniques for Functional and Structural Modeling of Nitrogenase
inferred← citeshttps://doi.org/10.1007/978-1-61779-194-9_2openalex-snapshot
Mechanism of Mo-Dependent Nitrogenase
inferred← citeshttps://doi.org/10.1007/978-3-030-24861-1_4openalex-snapshot
Electroactive Materials
inferred← citeshttps://doi.org/10.1007/978-3-030-90383-1_15openalex-snapshot
Marine Biogeochemical Cycles
inferred← citeshttps://doi.org/10.1007/978-3-319-30259-1_11openalex-snapshot
Why Is Planktonic Nitrogen Fixation So Rare in Coastal Marine Ecosystems? Insights from a Cross-Systems Approach
inferred← citeshttps://doi.org/10.1007/978-3-319-75103-0_2openalex-snapshot
Azolla: A Model System for Symbiotic Nitrogen Fixation and Evolutionary Developmental Biology
inferred← citeshttps://doi.org/10.1007/978-3-642-30141-4_72openalex-snapshot
Dinitrogen-Fixing Prokaryotes
inferred← citeshttps://doi.org/10.1007/978-3-642-37241-4_5openalex-snapshot
Plant-Associated Bacteria in Nitrogen Nutrition in Crops, with Special Reference to Rice and Banana
inferred← citeshttps://doi.org/10.1007/978-3-662-04064-5_5openalex-snapshot
Nodule Formation and Function
inferred← citeshttps://doi.org/10.1007/978-81-322-1880-7_14openalex-snapshot
Exploring the Genomes of Symbiotic Diazotrophs with Relevance to Biological Nitrogen Fixation
inferred← citeshttps://doi.org/10.1007/978-94-007-0388-9_6openalex-snapshot
Nitrogenases and Hydrogenases in Cyanobacteria
inferred← citeshttps://doi.org/10.1007/978-94-007-1533-2_15openalex-snapshot
The Physiology and Functional Genomics of Cyanobacterial Hydrogenases and Approaches Towards Biohydrogen Production
inferred← citeshttps://doi.org/10.1007/978-94-007-5479-9_3openalex-snapshot
Hydrogenases, Nitrogenases, Anoxia, and H2 Production in Water-Oxidizing Phototrophs
inferred← citeshttps://doi.org/10.1007/978-94-011-5159-7_16openalex-snapshot
The Fe-Only Nitrogenase From Rhodobacter capsulatus: 2. The FeFe Protein Metal Centers Probed by EXAFS and Mössbauer Spectroscopy
inferred← citeshttps://doi.org/10.1007/978-94-011-5159-7_3openalex-snapshot
Complex Structures of Nitrogenase
inferred← citeshttps://doi.org/10.1007/978-94-017-8554-9_12openalex-snapshot
Photosynthesis and Hydrogen Production in Purple Non Sulfur Bacteria: Fundamental and Applied Aspects
inferred← citeshttps://doi.org/10.1007/978-94-017-9269-1_7openalex-snapshot
Cleaving the N,N Triple Bond: The Transformation of Dinitrogen to Ammonia by Nitrogenases
inferred← citeshttps://doi.org/10.1007/978-981-10-7380-9_7openalex-snapshot
Biological Nitrogen Fixation in Cereals Crops: A Bacterial Perspective
inferred← citeshttps://doi.org/10.1007/978-981-10-7677-0_7openalex-snapshot
Hydrogen from Photo Fermentation
inferred← citeshttps://doi.org/10.1007/978-981-15-1902-4_16openalex-snapshot
Assessment of Genes and Enzymes of Microorganisms of High Altitudes and Their Application in Agriculture
inferred← citeshttps://doi.org/10.1007/bf02756066openalex-snapshot
Catalytic behavior of the nitrogenase iron-molybdenum cofactor extracted from the enzyme in the reduction of C2H2 under nonenzymatic conditions
inferred← citeshttps://doi.org/10.1007/s00027-021-00786-8openalex-snapshot
Trace metal and nitrogen concentrations differentially affect bloom forming cyanobacteria of the genus Dolichospermum
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