2,6-dichloroindophenol has been researched along with flavin-adenine dinucleotide in 11 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 4 (36.36) | 18.7374 |
| 1990's | 4 (36.36) | 18.2507 |
| 2000's | 3 (27.27) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Nishimura, M; Shioi, Y; Takamiya, K | 1 |
| Dancey, GF; Shapiro, BM | 1 |
| Fujii, K; Galivan, JH; Huennekens, FM | 1 |
| Oka, M; Tachibana, S | 1 |
| Dean, JF; Eriksson, KE; Habu, N; Samejima, M | 1 |
| de Vries, S; Duine, JA; Kim, SW; Luykx, DM | 1 |
| Bayer, M; Simon, H; Walter, K | 1 |
| Blasco, R; Castillo, F; Martínez-Luque, M | 1 |
| Ghisla, S; Golbik, R; Hübner, G; Tittmann, K | 1 |
| Pardo, JP; Velázquez, I | 1 |
| Basran, J; Finn, RD; Munro, AW; Paine, MJ; Roitel, O; Scrutton, NS; Wolf, CR | 1 |
11 other study(ies) available for 2,6-dichloroindophenol and flavin-adenine dinucleotide
| Article | Year |
|---|---|
Isolation and some properties of NAD+ reductase of the green photosynthetic bacterium Prosthecochloris aestuarii.
Topics: 2,6-Dichloroindophenol; Amobarbital; Bacteria; Benzyl Viologen; Ferredoxins; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Kinetics; Light; Molecular Weight; NADH, NADPH Oxidoreductases; NADPH-Ferrihemoprotein Reductase; Rotenone; Vitamin K | 1976 |
The NADH dehydrogenase of the respiratory chain of Escherichia coli. II. Kinetics of the purified enzyme and the effects of antibodies elicited against it on membrane-bound and free enzyme.
Topics: 2,6-Dichloroindophenol; Antibodies; Cell Membrane; Escherichia coli; Ferricyanides; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Immunodiffusion; Immunoelectrophoresis; Kinetics; NAD; NADH, NADPH Oxidoreductases; Oxygen Consumption; Vitamin K | 1976 |
Activation of methionine synthase: further characterization of flavoprotein system.
Topics: 2,6-Dichloroindophenol; 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase; Dithionite; Enzyme Activation; Escherichia coli; Ferricyanides; Flavin-Adenine Dinucleotide; Flavoproteins; Kinetics; Methyltransferases; NAD; NADP; Oxidation-Reduction; Paraquat; Vitamin K | 1977 |
A method for quantitation of vitamin B2 by using an enzyme (producing vitamin B2-aldehyde) from Schizophyllum commune.
Topics: 2,6-Dichloroindophenol; Agaricales; Alcohol Oxidoreductases; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Kinetics; Oxidation-Reduction; Phosphoric Monoester Hydrolases; Riboflavin; Schizophyllum | 1980 |
Release of the FAD domain from cellobiose oxidase by proteases from cellulolytic cultures of Phanerochaete chrysosporium.
Topics: 2,6-Dichloroindophenol; Animals; Basidiomycota; Blotting, Western; Carbohydrate Dehydrogenases; Cellulose; Cytochrome c Group; Electrophoresis, Polyacrylamide Gel; Flavin-Adenine Dinucleotide; Mice; Mice, Inbred BALB C; Phycomyces | 1993 |
A second molybdoprotein aldehyde dehydrogenase from Amycolatopsis methanolica NCIB 11946.
Topics: 2,6-Dichloroindophenol; Actinobacteria; Aldehyde Dehydrogenase; Binding Sites; Cytosine Nucleotides; Flavin-Adenine Dinucleotide; Iron; Macromolecular Substances; Protein Conformation; Pterins; Spectrophotometry; Substrate Specificity; Sulfides; Xanthine Oxidase | 1996 |
Purification and partial characterisation of a reversible artificial mediator accepting NADH oxidoreductase from Clostridium thermoaceticum.
Topics: 2,6-Dichloroindophenol; Amino Acid Sequence; Anthraquinones; Clostridium; Enzyme Stability; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Iron; Molecular Sequence Data; Molecular Weight; NAD; NADP Transhydrogenases; Paraquat; Sequence Analysis; Sequence Homology, Amino Acid; Spectrophotometry, Ultraviolet; Sulfur | 1996 |
The assimilatory nitrate reductase from the phototrophic bacterium, Rhodobacter capsulatus E1F1, is a flavoprotein.
Topics: 2,6-Dichloroindophenol; Cytochrome c Group; Dihydrolipoamide Dehydrogenase; Dimerization; Electron Transport; Electrophoresis, Polyacrylamide Gel; Flavin-Adenine Dinucleotide; Flavoproteins; Kinetics; Molecular Weight; NAD; Nitrate Reductase; Nitrate Reductases; Oxidation-Reduction; Protein Conformation; Rhodobacter capsulatus; Spectrophotometry | 1997 |
Mechanism of elementary catalytic steps of pyruvate oxidase from Lactobacillus plantarum.
Topics: 2,6-Dichloroindophenol; Buffers; Catalysis; Decarboxylation; Deuterium Oxide; Flavin-Adenine Dinucleotide; Kinetics; Lactobacillus; Oxidation-Reduction; Phosphates; Potassium Compounds; Pyruvate Oxidase; Pyruvic Acid; Solvents; Spectrophotometry; Substrate Specificity | 2000 |
Kinetic characterization of the rotenone-insensitive internal NADH: ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae.
Topics: 2,6-Dichloroindophenol; Adenosine Monophosphate; Binding, Competitive; Dose-Response Relationship, Drug; Electron Transport Complex I; Enzyme Activation; Enzyme Stability; Flavin-Adenine Dinucleotide; Flavones; Flavonoids; Hydrogen-Ion Concentration; Mitochondria; NAD; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Quinones; Rotenone; Saccharomyces cerevisiae | 2001 |
Determination of the redox potentials and electron transfer properties of the FAD- and FMN-binding domains of the human oxidoreductase NR1.
Topics: 2,6-Dichloroindophenol; Electron Transport; Ferricyanides; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; FMN Reductase; Humans; Oxidation-Reduction; Potentiometry; Protein Structure, Tertiary; Spectrum Analysis | 2003 |