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2,6-dichloroindophenol and quinone

2,6-dichloroindophenol has been researched along with quinone in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (75.00)18.2507
2000's1 (25.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Hirschberg, J; Ohad, N1
Dowd, SR; Felix, C; Ho, C; Hyde, JS; Sun, ZY1
Jouenne, T; Junter, GA; Tresse, O1
Banerjee, R; Munson, T; Olteanu, H1

Other Studies

4 other study(ies) available for 2,6-dichloroindophenol and quinone

ArticleYear
Mutations in the D1 subunit of photosystem II distinguish between quinone and herbicide binding sites.
    The Plant cell, 1992, Volume: 4, Issue:3

    Topics: 2,6-Dichloroindophenol; Amino Acid Sequence; Base Sequence; Benzoquinones; Binding Sites; Cyanobacteria; DNA; Drug Resistance; Herbicides; Molecular Sequence Data; Mutagenesis, Site-Directed; Photosynthesis; Photosynthetic Reaction Center Complex Proteins; Photosystem II Protein Complex; Polymerase Chain Reaction; Protein Conformation; Restriction Mapping; Sequence Homology, Nucleic Acid; Structure-Activity Relationship

1992
Stopped-flow kinetic and biophysical studies of membrane-associated D-lactate dehydrogenase of Escherichia coli.
    Biochimica et biophysica acta, 1995, Oct-25, Volume: 1252, Issue:2

    Topics: 2,6-Dichloroindophenol; Bacterial Outer Membrane Proteins; Benzoquinones; Electron Spin Resonance Spectroscopy; Escherichia coli; Kinetics; L-Lactate Dehydrogenase; Lactates; Lactic Acid; Magnetic Resonance Spectroscopy; Oxidation-Reduction; Spectrophotometry; Spin Labels

1995
Antibacterial efficacy of tobramycin against anaerobic Escherichia coli cultures in the presence of electron acceptors.
    The Journal of antimicrobial chemotherapy, 1997, Volume: 40, Issue:3

    Topics: 2,6-Dichloroindophenol; Anaerobiosis; Anti-Bacterial Agents; Benzoquinones; Biofilms; Electrons; Escherichia coli; Fumarates; Indicators and Reagents; Microbial Sensitivity Tests; Naphthoquinones; Tobramycin

1997
Differences in the efficiency of reductive activation of methionine synthase and exogenous electron acceptors between the common polymorphic variants of human methionine synthase reductase.
    Biochemistry, 2002, Nov-12, Volume: 41, Issue:45

    Topics: 2,6-Dichloroindophenol; 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase; Amino Acid Sequence; Animals; Benzoquinones; Electron Transport; Enzyme Activation; Ferredoxin-NADP Reductase; Ferricyanides; Free Radicals; Genetic Variation; Humans; Molecular Sequence Data; Mutagenesis, Site-Directed; NADP; Polymorphism, Genetic; Recombinant Fusion Proteins; Spectrophotometry, Ultraviolet; Swine

2002