Disease relevance of Dichlorophenolindophenol

• The purified respiratory chain NADH dehydrogenase of Escherichia coli oxidizes NADH with either dichlorophenolindophenol (DCIP). ferricyanide, or menadione as electron acceptors, with values for NADH are similar with the three electron acceptors (approximately 50 muM) [1].
• A novel nicotinoprotein, catalyzing the dichlorophenolindophenol-dependent oxidation of carveol to carvone, was purified to homogeneity from Rhodococcus erythropolis DCL14 [2].
• Addition of 5 microM 2,6-dichlorophenolindophenol, a hydrophobic electron-transfer mediator, to the assay mixture allowed susceptibility testing of a Gram-positive obligate anaerobe, Clostridium sporogenes [3].
• A combination of modified OF and DCIP tests should prove useful and applicable to prenatal screening programs for thalassemia and hemoglobinopathies in communities with limited facilities and economic resources [4].
• Primary screening for thalassemia and hemoglobinopathies usually involves an accurate blood count using an expensive electronic blood cell counter A cheaper alternative method was tested by using a modified osmotic fragility (OF) test and a modified dichlorophenolindophenol (DCIP) test [4].

High impact information on Dichlorophenolindophenol

• The enzyme kinetics of the purified heterodimer were studied with two two-electron acceptors, 2,6-dichloroindophenol and menadione, and a four-electron acceptor, methyl red, as the substrates [5].
• Measurements of thermoluminescence profiles and rates of reduction of 2,6-dichlorophenolindophenol indicated that PSII complexes in the mutant cells had functional reaction centers that were unable to accept electrons from water [6].
• We studied 10 colon carcinoma cell lines showing different levels of DTD activity (range, 0-3447 nmol/min/mg protein), as measured by the reduction of dichlorophenolindophenol [7].
• Glutamate (S1E) and aspartate (S1D) substitutions at site 1 resulted in the complete loss of PDC activity; however, these mutants were variably active in the decarboxylation and 2,6-dichlorophenolindophenol assays [8].
• The addition of Ca2+/calmodulin increased cytochrome c reduction from 10-15-fold while stimulating the rate of 2,6-dichlorophenolindophenol and ferricyanide reduction only slightly, if at all [9].

Chemical compound and disease context of Dichlorophenolindophenol

• Using a solution containing Escherichia coli O157, the electrochemical response with two different mediators [potassium hexacyanoferrate(III) and 2,6-dichlorophenolindophenol] was evaluated in the FIA system [10].
• Hydrogenase from Escherichia coli exhibited low activity when assayed for hydrogen:methyl viologen reductase activity and no activity when assayed for hydrogen-uptake activity with acceptors of high redox potential (dichloroindophenol, methylene blue) [11].
• The effects of magnesium and chloride ions on photosynthetic electron transport were investigated in membrane fragments of a blue-green alga, Nostoc muscorum (Strain 7119), noted for their stability and high rates of electron transport from water or reduced dichlorophenolindophenol to NADP+ [12].

Biological context of Dichlorophenolindophenol

• A complex designated Chla.P2, which was capable of electron transport from diphenylcarbazide to 2,6-dichlorophenolindophenol, was isolated by nondenaturing gel electrophoresis [13].
• It is most likely located on the surface of the protein at the cytochrome c/dichloroindophenol binding site, near the FMN prosthetic group [14].
• Oxidase activity as well as a phenylalanine-dichlorophenolindophenol (DCIP) reductase activity increased in P. mirabilis only during cell multiplication [15].
• Seven human and four murine tumor cell lines from different histological origins were evaluated for their DTD enzyme activity (evaluated using dichlorophenolindophenol and EO9 as substrates), DTD gene expression and chemosensitivity to EO9 [16].
• In the presence of reduced dichloroindophenol and absence of oxygen there is a marked inhibition of photophosphorylation [17].

Anatomical context of Dichlorophenolindophenol

• Inhibition of steroid hydroxylase activity by ferricyanide and dichlorophenolindophenol sulfonate was only observed in mitochondria which had been damaged by various techniques [18].
• The cluster was reconstituted by incubating the treated membranes with 1.0 mM Mn2+, 20 mM Ca2+, 10 microM 2,6-dichlorophenolindophenol, and Cl- under illumination with continuous or flashing light to restore the oxygen-evolving capacity [19].
• NADPH-dependent dichlorophenolindophenol (DCIP) reductase activity cosediments with NADPH-dependent O(2-)-generating activity in subcellular particulate fractions of zymosan-stimulated human polymorphonuclear leukocytes (PMN's) [20].
• Intrinsic dichlorophenolindophenol reductase activity associated with the superoxide-generating oxidoreductase of human granulocytes [20].
• In this investigation, extracellular reduction of 2,6-dichloroindophenol (DCIP) and ferricyanide (FeCN) were measured as indicators of trans-plasma membrane electron transport by chick forebrain neurons [21].

Associations of Dichlorophenolindophenol with other chemical compounds

• The dehydrogenase component abstracts electrons from the substrate and transfers them to oxidation-reduction dyes such as potassium ferricyanide and 2,6-dichlorophenolindophenol but not to molecular oxygen [22].
• Component B reduces several redox compounds: 2,6-dichlorophenolindophenol, potassium hexacyanoferrat III, cytochrome c, methylene blue, and nitro blue tetrazolium [23].
• Evidence for the presence of a flavin in the enzyme was drawn from these considerations: (a) the enzyme, while oxidatively cleaving saccharopine, concomitantly reduces 2,6-dichlorophenolindophenol; (b) the purified enzyme has a fluorescence spectrum typical of flavins; and (c) the enzyme requires oxygen and produces hydrogen peroxide [24].
• These reductions are inhibited by the thiol blocking agent N-ethylmaleimide and by the strong inhibitors of the thioredoxin reductase (TR) 2-chloro-2,4-nitrobenzene and 2,6-dichloroindophenol [25].
• Ascorbate in plasma as measured by liquid chromatography and by dichlorophenolindophenol colorimetry [26].

Gene context of Dichlorophenolindophenol

• The enzyme transferred electrons to cytochrome c, dichlorophenolindophenol, and nitro blue tetrazolium [27].
• The unique activity had properties of a diaphorase but was distinct from NQOI because of a lack of correlation between NQOI (2,6-dichlorophenolindophenol reduction) activity and the amount of MMC-reductive activation leading to DNA cross-linking [28].
• 2,6-Dichloroindophenol, which in previous studies was shown to be a good inhibitor of TR in vitro, was a poor inhibitor of TR in intact A204 cells and there was no significant correlation with inhibition of colony formation [29].
• Automated continuous-flow colorimetric determination of glutathione peroxidase with dichloroindophenol [30].
• The catalytic activities of ETFR and ETFB are comparable when they mediate the transfer of reducing equivalents between medium chain acyl-CoA dehydrogenase and 2,6-dichlorophenolindophenol [31].

Analytical, diagnostic and therapeutic context of Dichlorophenolindophenol

• FdIIint is observed during reductive titrations with dithionite or hydrogen/hydrogenase or after partial oxidation of FdIIR by 2,6-dichlorophenolindophenol or air [32].
• The reduced form of DCIP (DCIPH2) is measured amperometrically by flow-injection analysis [33].
• For each enzyme, the specificity of cleavage was determined by analytical HPLC while the kinetic constants were obtained from a kinetic assay involving a cellobiose dehydrogenase purified from H. insolens as a coupled enzyme using 2,6-dichloroindophenol as the electron acceptor [34].
• The core complex revealed electron-transfer activity (1,5-diphenylcarbazide----2,6-dichloroindophenol) of about 30 mumol reduced 2,6-dichloroindophenol/mg chlorophyll/h. The structural integrity was analyzed by electron microscopy [35].
• The enzyme is therefore called "ecdysone oxidase". Two methods are described for the detection of ecdysone oxidase activity, one using a radiolabelled substrate which is separated from the product by thin-layer chromatography after the reaction, and the other using dichloroindophenol, which is discoloured by the redox reaction [36].

References