Page last updated: 2024-08-17

histidine and guaiacol

histidine has been researched along with guaiacol in 8 studies

Research

Studies (8)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's5 (62.50)18.2507
2000's1 (12.50)29.6817
2010's2 (25.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Bandyopadhyay, U; Banerjee, RK; Bhattacharyya, DK1
de Montellano, PR; Newmyer, SL1
Loehr, TM; Newmyer, SL; Ortiz de Montellano, PR; Sun, J1
Ishimori, K; Morishima, I; Tanaka, M1
Kuo, JM; Ortiz de Montellano, PR; Savenkova, MI1
Canters, GW; Diederix, RE; Ubbink, M1
Aggrey-Fynn, JE; Surmeli, NB1
Du, KJ; Gao, SQ; Liao, F; Lin, YW; Liu, C; Tan, X; Wei, CW; Yuan, H1

Other Studies

8 other study(ies) available for histidine and guaiacol

ArticleYear
Chemical and kinetic evidence for an essential histidine residue in the electron transfer from aromatic donor to horseradish peroxidase compound I.
    The Journal of biological chemistry, 1993, Oct-25, Volume: 268, Issue:30

    Topics: Amino Acid Sequence; Binding Sites; Circular Dichroism; Computer Simulation; Diethyl Pyrocarbonate; Electron Transport; Guaiacol; Histidine; Horseradish Peroxidase; Hydrogen Peroxide; Hydrogen-Ion Concentration; Kinetics; Protein Conformation; Spectrophotometry

1993
Rescue of the catalytic activity of an H42A mutant of horseradish peroxidase by exogenous imidazoles.
    The Journal of biological chemistry, 1996, Jun-21, Volume: 271, Issue:25

    Topics: Binding Sites; Catalysis; Cloning, Molecular; Cyanides; Escherichia coli; Guaiacol; Heme; Histidine; Horseradish Peroxidase; Hydrogen-Ion Concentration; Imidazoles; Kinetics; Point Mutation; Recombinant Proteins; Sequence Tagged Sites; Spectrophotometry

1996
Rescue of the horseradish peroxidase His-170-->Ala mutant activity by imidazole: importance of proximal ligand tethering.
    Biochemistry, 1996, Oct-01, Volume: 35, Issue:39

    Topics: Baculoviridae; Benzothiazoles; Enzyme Activation; Escherichia coli; Guaiacol; Hemeproteins; Histidine; Horseradish Peroxidase; Hydrogen Peroxide; Hydrogen-Ion Concentration; Imidazoles; Iron; Kinetics; Mutation; Protein Binding; Recombinant Proteins; Spectrum Analysis, Raman; Sulfonic Acids

1996
The distal glutamic acid as an acid-base catalyst in the distal site of horseradish peroxidase.
    Biochemical and biophysical research communications, 1996, Oct-14, Volume: 227, Issue:2

    Topics: Amino Acid Sequence; Binding Sites; Chloride Peroxidase; Glutamic Acid; Guaiacol; Heme; Histidine; Horseradish Peroxidase; Hydrogen Peroxide; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Mutagenesis, Site-Directed; Oxidation-Reduction; Polymerase Chain Reaction; Recombinant Proteins; Spectrophotometry

1996
Improvement of peroxygenase activity by relocation of a catalytic histidine within the active site of horseradish peroxidase.
    Biochemistry, 1998, Jul-28, Volume: 37, Issue:30

    Topics: Alanine; Animals; Arginine; Benzothiazoles; Binding Sites; Catalysis; Cells, Cultured; Enzyme Activation; Guaiacol; Histidine; Horseradish Peroxidase; Hydrogen Peroxide; Kinetics; Mixed Function Oxygenases; Mutagenesis, Insertional; Recombinant Proteins; Spodoptera; Sulfonic Acids; Valine

1998
The peroxidase activity of cytochrome c-550 from Paracoccus versutus.
    European journal of biochemistry, 2001, Volume: 268, Issue:15

    Topics: Amino Acids; Catalysis; Cytochrome c Group; Dose-Response Relationship, Drug; Enzyme Activation; Guaiacol; Heme; Histidine; Horseradish Peroxidase; Hydrogen Peroxide; Hydrogen-Ion Concentration; Kinetics; Oxidation-Reduction; Paracoccus; Peroxidase; Protein Binding; Superoxide Dismutase; Superoxides; Time Factors

2001
A novel thermophilic hemoprotein scaffold for rational design of biocatalysts.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2018, Volume: 23, Issue:8

    Topics: Bacteria; Bacterial Proteins; Benzothiazoles; Biocatalysis; Guaiacol; Hemeproteins; Histidine; Hydrogen Peroxide; Hydrogen-Ion Concentration; Kinetics; Mutation; Peroxidases; Protein Engineering; Sulfonic Acids; Tyrosine

2018
Unique Tyr-heme double cross-links in F43Y/T67R myoglobin: an artificial enzyme with a peroxidase activity comparable to that of native peroxidases.
    Chemical communications (Cambridge, England), 2019, Jun-11, Volume: 55, Issue:46

    Topics: Animals; Arginine; Benzothiazoles; Biomimetic Materials; Guaiacol; Heme; Histidine; Hydrogen Peroxide; Hydrogen-Ion Concentration; Kinetics; Molecular Structure; Mutation; Myoglobin; Oxidation-Reduction; Peroxidases; Protein Processing, Post-Translational; Sperm Whale; Sulfonic Acids; Tyrosine

2019