hydroquinone and flavin mononucleotide

hydroquinone has been researched along with flavin mononucleotide in 10 studies

Research

Studies (10)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's6 (60.00)18.2507
2000's3 (30.00)29.6817
2010's0 (0.00)24.3611
2020's1 (10.00)2.80

Authors

AuthorsStudies
Geoghegan, SM; Mayhew, SG; O'Connell, DP; O'Farrell, PA; Yalloway, GN1
Mayhew, SG; O'Connell, DP; Yalloway, GN1
Curley, GP; Gallagher, ME; Malthouse, JP; Mayhew, SG; Yalloway, GN1
Bradley, LH; Swenson, RP2
Murataliev, MB1
Drennan, CL; Hoover, DM; Ludwig, ML; Metzger, AL; Osborne, C; Pattridge, KA; Weber, CH1
D'Arcy, D; Higgins, TM; Mayhew, SG; McCarthy, AA; O'Connell, DP; Reinhold, M; Verma, CS; Voordouw, G; Walsh, MA; Yalloway, GN1
Artenie, V; Brandsch, R; Chiribau, CB; Friedrich, T; Mihasan, M1
Chan, ACK; Do, LTM; McGregor, AK; Murphy, MEP; Saini, G; Schroeder, MD; Wolthers, KR1

Other Studies

10 other study(ies) available for hydroquinone and flavin mononucleotide

ArticleYear
Regulation of the redox potentials of flavodoxins: modification of the flavin binding.
    Biochemical Society transactions, 1996, Volume: 24, Issue:1

    Topics: Aspartic Acid; Binding Sites; Desulfovibrio vulgaris; Flavin Mononucleotide; Flavodoxin; Hydrogen-Ion Concentration; Hydroquinones; Mutagenesis, Site-Directed; Oxidation-Reduction; Point Mutation; Recombinant Proteins; Thermodynamics; Tryptophan; Tyrosine

1996
The effects of pH on the absorption spectrum of the hydroquinone of flavodoxin from Desulfovibrio vulgaris.
    Biochemical Society transactions, 1996, Volume: 24, Issue:1

    Topics: Desulfovibrio vulgaris; Flavin Mononucleotide; Flavodoxin; Hydrogen-Ion Concentration; Hydroquinones; Kinetics; Oxidation-Reduction; Spectrophotometry

1996
pH-dependent spectroscopic changes associated with the hydroquinone of FMN in flavodoxins.
    Biochemistry, 1999, Mar-23, Volume: 38, Issue:12

    Topics: Apoproteins; Desulfovibrio vulgaris; Flavin Mononucleotide; Flavodoxin; Hydrogen-Ion Concentration; Hydroquinones; Magnetic Resonance Spectroscopy; Mutation; Oxidation-Reduction

1999
Role of glutamate-59 hydrogen bonded to N(3)H of the flavin mononucleotide cofactor in the modulation of the redox potentials of the Clostridium beijerinckii flavodoxin. Glutamate-59 is not responsible for the pH dependency but contributes to the stabiliz
    Biochemistry, 1999, Sep-21, Volume: 38, Issue:38

    Topics: Circular Dichroism; Clostridium; Coenzymes; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Flavodoxin; Glutamic Acid; Glutamine; Hydrogen Bonding; Hydrogen-Ion Concentration; Hydroquinones; Mutagenesis, Site-Directed; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Protein Binding; Protons; Spectrophotometry, Ultraviolet; Temperature; Thermodynamics

1999
Application of electron spin resonance (ESR) for detection and characterization of flavoprotein semiquinones.
    Methods in molecular biology (Clifton, N.J.), 1999, Volume: 131

    Topics: Catalysis; Electron Spin Resonance Spectroscopy; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Flavoproteins; Glucose Oxidase; Hydroquinones; Oxidation-Reduction; Quinones

1999
Comparisons of wild-type and mutant flavodoxins from Anacystis nidulans. Structural determinants of the redox potentials.
    Journal of molecular biology, 1999, Dec-03, Volume: 294, Issue:3

    Topics: Amino Acid Sequence; Binding Sites; Crystallography, X-Ray; Cyanobacteria; Escherichia coli; Flavin Mononucleotide; Flavodoxin; Hydroquinones; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Peptides; Sequence Alignment; Structure-Activity Relationship

1999
Role of hydrogen bonding interactions to N(3)H of the flavin mononucleotide cofactor in the modulation of the redox potentials of the Clostridium beijerinckii flavodoxin.
    Biochemistry, 2001, Jul-31, Volume: 40, Issue:30

    Topics: Amino Acid Substitution; Binding Sites; Clostridium; Flavin Mononucleotide; Flavodoxin; Glutamic Acid; Hydrogen Bonding; Hydroquinones; Models, Chemical; Mutagenesis, Site-Directed; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Potentiometry; Protons; Temperature; Thermodynamics

2001
Crystallographic investigation of the role of aspartate 95 in the modulation of the redox potentials of Desulfovibrio vulgaris flavodoxin.
    Biochemistry, 2002, Sep-10, Volume: 41, Issue:36

    Topics: Alanine; Amino Acid Substitution; Aspartic Acid; Binding Sites; Computer Simulation; Crystallography, X-Ray; Desulfovibrio vulgaris; Flavin Mononucleotide; Flavodoxin; Glutamic Acid; Hydrogen Bonding; Hydroquinones; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Conformation; Protein Structure, Secondary; Static Electricity; Thermodynamics

2002
An NAD(P)H-nicotine blue oxidoreductase is part of the nicotine regulon and may protect Arthrobacter nicotinovorans from oxidative stress during nicotine catabolism.
    Applied and environmental microbiology, 2007, Volume: 73, Issue:8

    Topics: Arthrobacter; Cloning, Molecular; Coenzymes; Electron Spin Resonance Spectroscopy; Flavin Mononucleotide; Gene Expression Regulation, Bacterial; Hydroquinones; Models, Biological; NAD; NADP; Nicotine; Oxidation-Reduction; Oxidative Stress; Quinone Reductases; Regulon; RNA, Bacterial; RNA, Messenger; Substrate Specificity

2007
A new member of the flavodoxin superfamily from Fusobacterium nucleatum that functions in heme trafficking and reduction of anaerobilin.
    The Journal of biological chemistry, 2023, Volume: 299, Issue:7

    Topics: Bacterial Proteins; Biological Transport; Flavin Mononucleotide; Flavodoxin; Fusobacterium Infections; Fusobacterium nucleatum; Genes, Bacterial; Heme; Humans; Iron; Oxidation-Reduction; Protein Domains; Tetrapyrroles

2023