2,6-dichloroindophenol has been researched along with flavin mononucleotide in 13 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 8 (61.54) | 18.7374 |
| 1990's | 3 (23.08) | 18.2507 |
| 2000's | 2 (15.38) | 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 |
| Jorns, MS | 1 |
| Canevascini, G; Eberhardt, U | 1 |
| Lingens, F; Markus, A; Ruf, HH; Schweizer, D; Seez, M | 1 |
| Oka, M; Tachibana, S | 1 |
| Arceneaux, JE; Byers, BR; Gaines, CG; Lodge, JS | 1 |
| Jorns, MS; Meyers, RD | 1 |
| Buswell, JA; Mains, I; Power, DM; Thomas, EW | 1 |
| Fujii, S; Kuroda, K; Miura, R; Yamano, T | 1 |
| Bayer, M; Simon, H; Walter, K | 1 |
| Abu-Soud, HM; Adak, S; Ghosh, S; Stuehr, DJ | 1 |
| Basran, J; Finn, RD; Munro, AW; Paine, MJ; Roitel, O; Scrutton, NS; Wolf, CR | 1 |
| Dass, VR; Jamakhandi, AP; Jeffus, BC; Miller, GP | 1 |
13 other study(ies) available for 2,6-dichloroindophenol and flavin mononucleotide
| 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 |
Glycolic acid oxidase from pig liver.
Topics: 2,6-Dichloroindophenol; Alcohol Oxidoreductases; Animals; Binding Sites; Chromatography, DEAE-Cellulose; Chromatography, Ion Exchange; Drug Stability; Ferricyanides; Flavin Mononucleotide; Glycolates; Kinetics; Liver; Methods; Molecular Weight; Spectrophotometry; Spectrophotometry, Ultraviolet; Swine | 1975 |
Chemolithotrophic growth and regulation of hydrogenase formation in the coryneform hydrogen bacterium strain 11/x.
Topics: 2,6-Dichloroindophenol; Acetates; Actinomycetales; Carbon Dioxide; Cell-Free System; Culture Media; Enzyme Induction; Enzyme Repression; Flavin Mononucleotide; Fructose; Gluconates; Glucose; Glutamates; Hydrogen; Mannitol; Methylene Blue; Methylphenazonium Methosulfate; Oxidoreductases; Oxygen Consumption; Ribulose-Bisphosphate Carboxylase; Species Specificity; Vitamin K | 1975 |
Purification and some properties of component B of the 4-chlorophenylacetate 3,4-dioxygenase from Pseudomonas species strain CBS 3.
Topics: 2,6-Dichloroindophenol; Amino Acids; Cytochrome c Group; Dioxygenases; Electron Spin Resonance Spectroscopy; Flavin Mononucleotide; Isoelectric Point; Kinetics; Macromolecular Substances; Molecular Weight; NAD; Oxygenases; Pseudomonas | 1987 |
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 |
Ferrisiderophore reductase activity associated with an aromatic biosynthetic enzyme complex in Bacillus subtilis.
Topics: 2,6-Dichloroindophenol; Bacillus subtilis; Cations, Divalent; Chorismic Acid; Flavin Mononucleotide; Hydroxybenzoates; Iron Chelating Agents; Lyases; NADH, NADPH Oxidoreductases; Oxidoreductases; Phosphorus-Oxygen Lyases; Quinic Acid | 1981 |
Identification of the factor responsible for autogenous bleaching of glycollate oxidase.
Topics: 2,6-Dichloroindophenol; Alcohol Oxidoreductases; Animals; Flavin Mononucleotide; Hydrogen Peroxide; Kinetics; Liver; Oxidation-Reduction; Spectrophotometry; Sulfites; Swine | 1981 |
Purification of an NADH-(dichlorophenol-indophenol) oxidoreductase from Bacillus stearothermophilus.
Topics: 2,6-Dichloroindophenol; Chromatography, Liquid; Cytochrome Reductases; Enzyme Activation; Flavin Mononucleotide; Geobacillus stearothermophilus; Methods; NADH Dehydrogenase; Potassium Cyanide | 1980 |
Characterization of the electron acceptors of old yellow enzyme: mechanistic approach to the mode of one electron transfer from the enzyme to menadione or dyestuffs.
Topics: 2,6-Dichloroindophenol; Cyclic N-Oxides; Cytochrome c Group; Electron Transport; Flavin Mononucleotide; Methylene Blue; NADP; NADPH Dehydrogenase; Nitrogen Oxides; Oxidation-Reduction; Oxygen Consumption; Spectrometry, Fluorescence; Spin Labels; Vitamin K | 1993 |
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 |
Role of reductase domain cluster 1 acidic residues in neuronal nitric-oxide synthase. Characterization of the FMN-FREE enzyme.
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 |
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 |
Thermal inactivation of the reductase domain of cytochrome P450 BM3.
Topics: 2,6-Dichloroindophenol; Bacterial Proteins; Biochemistry; Buffers; Catalysis; Cross-Linking Reagents; Cytochrome P-450 Enzyme System; Cytochromes c; Dimerization; Enzyme Activation; Flavin Mononucleotide; Mixed Function Oxygenases; NADPH-Ferrihemoprotein Reductase; Osmolar Concentration; Phosphates; Protein Denaturation; Protein Structure, Tertiary; Temperature | 2005 |