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dithionitrobenzoic acid and flavin-adenine dinucleotide

dithionitrobenzoic acid has been researched along with flavin-adenine dinucleotide in 15 studies

Research

Studies (15)

TimeframeStudies, this research(%)All Research%
pre-19905 (33.33)18.7374
1990's5 (33.33)18.2507
2000's3 (20.00)29.6817
2010's2 (13.33)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Kurebayashi, H; Nakamura, M; Yamazaki, I1
Castillo, F; de la Rosa, FF; Palacián, E1
Gaal, A; Neujahr, HY1
Seto, B; Stadtman, TC1
Cabré, F; Canela, EI; Cascante, M1
Ichikawa, Y; Ohnishi, T; Yamazaki, M1
Bichler, V; Brandsch, R1
Katsume, T; Muratsubaki, H1
Liu, SY; Stadtman, TC1
Mulrooney, SB; Veine, DM; Wang, PF; Williams, CH1
Bar-Noy, S; Gorlatov, SN; Stadtman, TC1
Poole, LB; Reynolds, CM1
Dick, S; Frey, HE; Lepock, JR; Siemann, S; Viswanatha, T1
Ma, K; Yang, X1
Gadhave, K; Giri, R; Kalita, P; Shukla, H; Tripathi, T1

Other Studies

15 other study(ies) available for dithionitrobenzoic acid and flavin-adenine dinucleotide

ArticleYear
One-electron and two-electron reductions of acceptors by xanthine oxidase and xanthine dehydrogenase.
    Journal of biochemistry, 1978, Volume: 83, Issue:1

    Topics: Chloromercuribenzoates; Dithionitrobenzoic Acid; Electron Transport; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Ketone Oxidoreductases; NAD; Oxygen; Quinones; Sulfhydryl Compounds; Xanthine Dehydrogenase; Xanthine Oxidase

1978
Nitrate reductase from Spinacea oleracea. Effects of sulfhydryl-group reagents on the activities of the complex and the inactivation by NADH.
    Biochemical and biophysical research communications, 1975, May-19, Volume: 64, Issue:2

    Topics: Dithioerythritol; Dithionitrobenzoic Acid; Dose-Response Relationship, Drug; Ethylmaleimide; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Hydroxymercuribenzoates; Iodoacetates; NAD; Nitrate Reductases; Plants; Sulfhydryl Reagents

1975
Phenol hydroxylase from yeast. Sulfhydryl groups in phenol hydroxylase from Trichosporon cutaneum.
    European journal of biochemistry, 1975, Oct-15, Volume: 58, Issue:2

    Topics: Apoenzymes; Dithionitrobenzoic Acid; Dithiothreitol; Edetic Acid; Flavin-Adenine Dinucleotide; Hydroxymercuribenzoates; Mercaptoethanol; Mitosporic Fungi; Mixed Function Oxygenases; Molecular Weight; Phenols; Sulfhydryl Compounds

1975
Purification and properties of proline reductase from Clostridium sticklandii.
    The Journal of biological chemistry, 1976, Apr-25, Volume: 251, Issue:8

    Topics: Amino Acid Oxidoreductases; Amino Acids; Cell Membrane; Clostridium; Dithionitrobenzoic Acid; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Macromolecular Substances; Molecular Weight; Protein Conformation; Spectrophotometry, Ultraviolet

1976
The molybdoenzymes xanthine oxidase and aldehyde oxidase contain fast- and slow-DTNB reacting sulphydryl groups.
    Journal of protein chemistry, 1992, Volume: 11, Issue:5

    Topics: Aldehyde Oxidase; Aldehyde Oxidoreductases; Animals; Binding Sites; Cattle; Dithionitrobenzoic Acid; Flavin-Adenine Dinucleotide; Kinetics; Oxidation-Reduction; Protein Denaturation; Sulfhydryl Compounds; Xanthine Oxidase

1992
Selective chemical modification of amino acid residues in the flavin adenine dinucleotide binding site of NADPH-ferredoxin reductase.
    The International journal of biochemistry, 1992, Volume: 24, Issue:2

    Topics: Amino Acid Sequence; Amino Acids; Animals; Binding Sites; Cattle; Diethyl Pyrocarbonate; Dithionitrobenzoic Acid; Ferredoxin-NADP Reductase; Flavin-Adenine Dinucleotide; Fluorescence; Kinetics; Molecular Sequence Data

1992
Autoflavinylation of apo6-hydroxy-D-nicotine oxidase.
    The Journal of biological chemistry, 1991, Oct-05, Volume: 266, Issue:28

    Topics: Amino Acid Sequence; Anaerobiosis; beta-Galactosidase; Catalysis; Cloning, Molecular; Dithionitrobenzoic Acid; Flavin-Adenine Dinucleotide; Glycerol; Kinetics; Molecular Sequence Data; Molecular Structure; Oxidoreductases; Recombinant Fusion Proteins; Temperature

1991
Characterization of fumarate reductase from baker's yeast: essential sulfhydryl group for binding of FAD.
    Journal of biochemistry, 1985, Volume: 97, Issue:4

    Topics: Apoenzymes; Cysteine; Dithionitrobenzoic Acid; Flavin-Adenine Dinucleotide; Kinetics; Saccharomyces cerevisiae; Succinate Dehydrogenase

1985
Heparin-binding properties of selenium-containing thioredoxin reductase from HeLa cells and human lung adenocarcinoma cells.
    Proceedings of the National Academy of Sciences of the United States of America, 1997, Jun-10, Volume: 94, Issue:12

    Topics: Adenocarcinoma; Amino Acid Sequence; Base Sequence; Binding Sites; Chromatography, Affinity; Chromatography, Gel; Chromatography, High Pressure Liquid; Dithionitrobenzoic Acid; Electrophoresis, Polyacrylamide Gel; Flavin-Adenine Dinucleotide; HeLa Cells; Heparin; Humans; Kinetics; Lung Neoplasms; Peptide Fragments; Placenta; Selenium; Selenocysteine; Thioredoxin-Disulfide Reductase; Tumor Cells, Cultured

1997
Formation and properties of mixed disulfides between thioredoxin reductase from Escherichia coli and thioredoxin: evidence that cysteine-138 functions to initiate dithiol-disulfide interchange and to accept the reducing equivalent from reduced flavin.
    Protein science : a publication of the Protein Society, 1998, Volume: 7, Issue:6

    Topics: Cysteine; Disulfides; Dithionite; Dithionitrobenzoic Acid; Dithiothreitol; Escherichia coli; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Mutagenesis, Site-Directed; NADP; Osmolar Concentration; Oxidation-Reduction; Protein Conformation; Protein Engineering; Spectrometry, Fluorescence; Structure-Activity Relationship; Sulfhydryl Compounds; Thioredoxin-Disulfide Reductase; Thioredoxins

1998
Overexpression of wild type and SeCys/Cys mutant of human thioredoxin reductase in E. coli: the role of selenocysteine in the catalytic activity.
    Free radical biology & medicine, 2001, Jan-01, Volume: 30, Issue:1

    Topics: Animals; Catalysis; Chemical Phenomena; Chemistry, Physical; Chromatography, High Pressure Liquid; Codon; Dimerization; Dithionitrobenzoic Acid; Escherichia coli; Flavin-Adenine Dinucleotide; Formate Dehydrogenases; Gene Expression; Humans; Hydrogenase; Kinetics; Multienzyme Complexes; Mutation; NADP; Rats; Recombinant Proteins; Selenium; Selenocysteine; Solubility; Structure-Activity Relationship; Substrate Specificity; Thioredoxin-Disulfide Reductase

2001
Activity of one of two engineered heterodimers of AhpF, the NADH:peroxiredoxin oxidoreductase from Salmonella typhimurium, reveals intrasubunit electron transfer between domains.
    Biochemistry, 2001, Apr-03, Volume: 40, Issue:13

    Topics: Catalysis; Dimerization; Dithionitrobenzoic Acid; Electron Transport; Enzyme Activation; Flavin-Adenine Dinucleotide; Flavins; Mutagenesis, Site-Directed; NAD; Oxidation-Reduction; Peptide Fragments; Peroxidases; Peroxiredoxins; Plasmids; Protein Structure, Tertiary; Salmonella typhimurium; Spectrometry, Fluorescence; Spectrophotometry

2001
Recombinant lysine:N(6)-hydroxylase: effect of cysteine-->alanine replacements on structural integrity and catalytic competence.
    Biochimica et biophysica acta, 2002, Feb-11, Volume: 1594, Issue:2

    Topics: Alanine; Calorimetry, Differential Scanning; Cysteine; Dithionitrobenzoic Acid; Enzyme Stability; Flavin-Adenine Dinucleotide; Hot Temperature; Iopanoic Acid; Kinetics; Mixed Function Oxygenases; Models, Chemical; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Conformation; Recombinant Proteins

2002
Characterization of a thioredoxin-thioredoxin reductase system from the hyperthermophilic bacterium Thermotoga maritima.
    Journal of bacteriology, 2010, Volume: 192, Issue:5

    Topics: Animals; Benzyl Viologen; Cattle; Coenzymes; Dimerization; Dithionitrobenzoic Acid; Electrophoresis, Polyacrylamide Gel; Enzyme Stability; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Insulin; Kinetics; Molecular Weight; NAD; NADP; Oxidation-Reduction; Sequence Homology, Amino Acid; Temperature; Thermotoga maritima; Thioredoxin-Disulfide Reductase; Thioredoxins

2010
Role of the glutaredoxin domain and FAD in the stabilization of thioredoxin glutathione reductase.
    Archives of biochemistry and biophysics, 2018, 10-15, Volume: 656

    Topics: Animals; Catalysis; Dithionitrobenzoic Acid; Fasciola; Flavin-Adenine Dinucleotide; Glutaredoxins; Helminth Proteins; Multienzyme Complexes; Mutation; NADH, NADPH Oxidoreductases; NADP; Protein Binding; Protein Conformation; Protein Domains; Protein Stability; Protein Unfolding; Thioredoxins; Tryptophan; Urea

2018