histidine has been researched along with guaiacol in 8 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 5 (62.50) | 18.2507 |
2000's | 1 (12.50) | 29.6817 |
2010's | 2 (25.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Bandyopadhyay, U; Banerjee, RK; Bhattacharyya, DK | 1 |
de Montellano, PR; Newmyer, SL | 1 |
Loehr, TM; Newmyer, SL; Ortiz de Montellano, PR; Sun, J | 1 |
Ishimori, K; Morishima, I; Tanaka, M | 1 |
Kuo, JM; Ortiz de Montellano, PR; Savenkova, MI | 1 |
Canters, GW; Diederix, RE; Ubbink, M | 1 |
Aggrey-Fynn, JE; Surmeli, NB | 1 |
Du, KJ; Gao, SQ; Liao, F; Lin, YW; Liu, C; Tan, X; Wei, CW; Yuan, H | 1 |
8 other study(ies) available for histidine and guaiacol
Article | Year |
---|---|
Chemical and kinetic evidence for an essential histidine residue in the electron transfer from aromatic donor to horseradish peroxidase compound I.
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.
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.
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.
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.
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.
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.
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.
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 |