Page last updated: 2024-08-17

lysine and nitrogenase

lysine has been researched along with nitrogenase in 7 studies

Research

Studies (7)

TimeframeStudies, this research(%)All Research%
pre-19901 (14.29)18.7374
1990's5 (71.43)18.2507
2000's1 (14.29)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Dean, DR; Morgan, TV; Mortenson, LE; Seefeldt, LC1
Lee, JC; Timasheff, SN1
Seefeldt, LC1
Lanzilotta, WN; Mortenson, LE; Ryle, MJ; Seefeldt, LC; Watt, GD1
Drummond, M; Green, A; Huff, S1
Johnson, MK; Lafferty, ME; Lou, J; Maier, RJ; Miller, A; Moshiri, F; Sorkin, DL1
Bröcker, MJ; Ganskow, S; Heathcote, P; Heinz, DW; Jahn, D; Moser, J; Schubert, WD; Virus, S1

Other Studies

7 other study(ies) available for lysine and nitrogenase

ArticleYear
Mapping the site(s) of MgATP and MgADP interaction with the nitrogenase of Azotobacter vinelandii. Lysine 15 of the iron protein plays a major role in MgATP interaction.
    The Journal of biological chemistry, 1992, Apr-05, Volume: 267, Issue:10

    Topics: Adenosine Diphosphate; Adenosine Triphosphate; Amino Acid Sequence; Azotobacter vinelandii; Bacterial Proteins; Base Sequence; Blotting, Western; Cross-Linking Reagents; Electron Spin Resonance Spectroscopy; Electrophoresis, Polyacrylamide Gel; Kinetics; Lysine; Metalloproteins; Molecular Sequence Data; Mutagenesis, Site-Directed; Nitrogenase; Nonheme Iron Proteins; Plasmids

1992
The calculation of partial specific volumes of proteins in guanidine hydrochloride.
    Archives of biochemistry and biophysics, 1974, Volume: 165, Issue:1

    Topics: Actins; Amino Acid Oxidoreductases; Amino Acids; Animals; Binding Sites; Blood Platelets; Carboxy-Lyases; Cattle; Chymotrypsinogen; Escherichia coli; Esterases; Guanidines; Liver; Lysine; Malate Dehydrogenase; Mathematics; Myocardium; Nitrogenase; Phosphopyruvate Hydratase; Protein Binding; Protein Conformation; Protein Denaturation; Proteins; Swine; Thiobacillus

1974
Docking of nitrogenase iron- and molybdenum-iron proteins for electron transfer and MgATP hydrolysis: the role of arginine 140 and lysine 143 of the Azotobacter vinelandii iron protein.
    Protein science : a publication of the Protein Society, 1994, Volume: 3, Issue:11

    Topics: Adenosine Triphosphate; Arginine; Azotobacter vinelandii; Chelating Agents; Electron Transport; Glutamic Acid; Hydrolysis; Kinetics; Lysine; Models, Molecular; Molybdoferredoxin; Mutagenesis, Site-Directed; Nitrogenase; Oxidoreductases; Point Mutation; Protein Structure, Tertiary; Sodium Chloride

1994
Evidence for a central role of lysine 15 of Azotobacter vinelandii nitrogenase iron protein in nucleotide binding and protein conformational changes.
    The Journal of biological chemistry, 1995, Jun-02, Volume: 270, Issue:22

    Topics: Adenosine Diphosphate; Adenosine Triphosphate; Amino Acid Sequence; Azotobacter vinelandii; Lysine; Molecular Sequence Data; Nitrogenase; Oxidoreductases; Protein Binding; Protein Conformation

1995
Roulette mutagenesis of the FMN-binding site of Klebsiella pneumoniae flavodoxin.
    European journal of biochemistry, 1993, Oct-01, Volume: 217, Issue:1

    Topics: Amino Acid Sequence; Base Sequence; Binding Sites; Codon; Flavin Mononucleotide; Flavodoxin; Glycine; Klebsiella pneumoniae; Lysine; Molecular Sequence Data; Mutagenesis; Nitrogenase; Phenotype; Protein Structure, Secondary; Threonine

1993
Mutagenesis studies of the FeSII protein of Azotobacter vinelandii: roles of histidine and lysine residues in the protection of nitrogenase from oxygen damage.
    Biochemistry, 1999, Apr-27, Volume: 38, Issue:17

    Topics: Azotobacter vinelandii; Bacterial Proteins; Carrier Proteins; Enzyme Activation; Escherichia coli; Histidine; Iron-Sulfur Proteins; Lysine; Mutagenesis, Site-Directed; Nitrogenase; Oxygen; Recombinant Proteins

1999
ATP-driven reduction by dark-operative protochlorophyllide oxidoreductase from Chlorobium tepidum mechanistically resembles nitrogenase catalysis.
    The Journal of biological chemistry, 2008, Apr-18, Volume: 283, Issue:16

    Topics: Adenosine Triphosphate; Catalysis; Chlorobium; Cysteine; Dithionite; Electrons; Escherichia coli; Heme; Kinetics; Leucine; Light; Lysine; Nitrogenase; Oxidoreductases; Protochlorophyllide

2008