glutamic acid and flavin mononucleotide

glutamic acid has been researched along with flavin mononucleotide in 11 studies

Research

Studies (11)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (27.27)18.2507
2000's6 (54.55)29.6817
2010's1 (9.09)24.3611
2020's1 (9.09)2.80

Authors

AuthorsStudies
Curti, B; Edmondson, DE; Fischer, F; Hagen, WR; Ravasio, S; Vanoni, MA; Verzotti, E; Zanetti, G1
Abu-Soud, HM; Adak, S; Ghosh, S; Stuehr, DJ1
Bradley, LH; Swenson, RP2
Candau, P; Florencio, FJ; Martín-Figueroa, E; Navarro, F1
Kasim, M; Swenson, RP1
D'Arcy, D; Higgins, TM; Mayhew, SG; McCarthy, AA; O'Connell, DP; Reinhold, M; Verma, CS; Voordouw, G; Walsh, MA; Yalloway, GN1
Hosseinkhani, S; Meighen, EA; Szittner, R1
Eissa, NT; Getzoff, ED; Liu, XD; Mazumdar, T; Xu, Y1
Belevich, G; Bloch, DA; Knuuti, J; Sharma, V; Verkhovskaya, M1
Anstöter, CS; Dessent, CEH; Uleanya, KO1

Other Studies

11 other study(ies) available for glutamic acid and flavin mononucleotide

ArticleYear
The recombinant alpha subunit of glutamate synthase: spectroscopic and catalytic properties.
    Biochemistry, 1998, Feb-17, Volume: 37, Issue:7

    Topics: Azospirillum brasilense; Bacterial Proteins; Catalysis; Flavin Mononucleotide; Glutamate Synthase; Glutamic Acid; Glutaminase; Recombinant Proteins; Spectrophotometry

1998
Role of reductase domain cluster 1 acidic residues in neuronal nitric-oxide synthase. Characterization of the FMN-FREE enzyme.
    The Journal of biological chemistry, 1999, Aug-06, Volume: 274, Issue:32

    Topics: 2,6-Dichloroindophenol; Amino Acid Sequence; Amino Acids, Dicarboxylic; Aspartic Acid; Calmodulin; Conserved Sequence; Cytochrome c Group; Electron Transport; Enzyme Activation; Ferricyanides; Flavin Mononucleotide; Flavoproteins; Fluorescence; Glutamic Acid; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Nerve Tissue Proteins; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Sequence Homology, Amino Acid

1999
Role of glutamate-59 hydrogen bonded to N(3)H of the flavin mononucleotide cofactor in the modulation of the redox potentials of the Clostridium beijerinckii flavodoxin. Glutamate-59 is not responsible for the pH dependency but contributes to the stabiliz
    Biochemistry, 1999, Sep-21, Volume: 38, Issue:38

    Topics: Circular Dichroism; Clostridium; Coenzymes; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Flavodoxin; Glutamic Acid; Glutamine; Hydrogen Bonding; Hydrogen-Ion Concentration; Hydroquinones; Mutagenesis, Site-Directed; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Protein Binding; Protons; Spectrophotometry, Ultraviolet; Temperature; Thermodynamics

1999
Ferredoxin-dependent iron-sulfur flavoprotein glutamate synthase (GlsF) from the Cyanobacterium synechocystis sp. PCC 6803: expression and assembly in Escherichia coli.
    Archives of biochemistry and biophysics, 2000, Jul-15, Volume: 379, Issue:2

    Topics: Amino Acid Oxidoreductases; Amino Acid Sequence; Cyanobacteria; Electron Spin Resonance Spectroscopy; Escherichia coli; Ferredoxins; Flavin Mononucleotide; Flavins; Flavoproteins; Genetic Complementation Test; Glutamic Acid; Iron; Kinetics; Oxidation-Reduction; Recombinant Proteins; Sequence Analysis, Protein; Spectrophotometry; Substrate Specificity; Sulfides

2000
Role of hydrogen bonding interactions to N(3)H of the flavin mononucleotide cofactor in the modulation of the redox potentials of the Clostridium beijerinckii flavodoxin.
    Biochemistry, 2001, Jul-31, Volume: 40, Issue:30

    Topics: Amino Acid Substitution; Binding Sites; Clostridium; Flavin Mononucleotide; Flavodoxin; Glutamic Acid; Hydrogen Bonding; Hydroquinones; Models, Chemical; Mutagenesis, Site-Directed; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Potentiometry; Protons; Temperature; Thermodynamics

2001
Alanine-scanning of the 50's loop in the Clostridium beijerinckii flavodoxin: evaluation of additivity and the importance of interactions provided by the main chain in the modulation of the oxidation-reduction potentials.
    Biochemistry, 2001, Nov-13, Volume: 40, Issue:45

    Topics: Alanine; Amino Acid Substitution; Clostridium; Flavin Mononucleotide; Flavodoxin; Glutamic Acid; Methionine; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Structure, Secondary

2001
Crystallographic investigation of the role of aspartate 95 in the modulation of the redox potentials of Desulfovibrio vulgaris flavodoxin.
    Biochemistry, 2002, Sep-10, Volume: 41, Issue:36

    Topics: Alanine; Amino Acid Substitution; Aspartic Acid; Binding Sites; Computer Simulation; Crystallography, X-Ray; Desulfovibrio vulgaris; Flavin Mononucleotide; Flavodoxin; Glutamic Acid; Hydrogen Bonding; Hydroquinones; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Conformation; Protein Structure, Secondary; Static Electricity; Thermodynamics

2002
Random mutagenesis of bacterial luciferase: critical role of Glu175 in the control of luminescence decay.
    The Biochemical journal, 2005, Jan-15, Volume: 385, Issue:Pt 2

    Topics: Aldehydes; Bacterial Proteins; Cloning, Molecular; Flavin Mononucleotide; Flavins; Glutamic Acid; Luciferases, Bacterial; Luminescence; Luminescent Measurements; Luminescent Proteins; Models, Chemical; Mutagenesis; Photobacterium; Photorhabdus; Research Design; Substrate Specificity; Vibrio

2005
Identification of a flavin mononucleotide module residue critical for activity of inducible nitrite oxide synthase.
    Journal of immunology (Baltimore, Md. : 1950), 2009, Nov-01, Volume: 183, Issue:9

    Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Aspartic Acid; Cell Line; Dimerization; Enzyme Activation; Flavin Mononucleotide; Glutamic Acid; Humans; Mice; Molecular Sequence Data; Mutagenesis, Site-Directed; Nitric Oxide; Nitric Oxide Synthase Type II; Protein Conformation; Protein Structure, Tertiary

2009
A single amino acid residue controls ROS production in the respiratory Complex I from Escherichia coli.
    Molecular microbiology, 2013, Volume: 90, Issue:6

    Topics: Catalytic Domain; Electron Transport Complex I; Escherichia coli; Escherichia coli Proteins; Flavin Mononucleotide; Glutamic Acid; Models, Molecular; Mutation; NAD; Oxidation-Reduction; Oxygen; Protein Binding; Quinone Reductases; Reactive Oxygen Species; Ubiquinone

2013
Photodissociative decay pathways of the flavin mononucleotide anion and its complexes with tryptophan and glutamic acid.
    Physical chemistry chemical physics : PCCP, 2023, Nov-15, Volume: 25, Issue:44

    Topics: Anions; Flavin Mononucleotide; Glutamic Acid; Protons; Tryptophan

2023