heme has been researched along with benzohydroxamic acid in 17 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 7 (41.18) | 18.2507 |
| 2000's | 9 (52.94) | 29.6817 |
| 2010's | 1 (5.88) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Dugad, LB; Goff, HM | 1 |
| Bray, RC; Burke, JF; Sanders, SA; Smith, AT; Thorneley, RN; Veitch, NC; Williams, RJ | 1 |
| Day, EP; Pearce, LL; Peterson, J; Wilson, MT | 1 |
| Gilfoyle, DJ; Rodriguez-Lopez, JN; Smith, AT | 1 |
| Gao, Y; Smith, AT; Veitch, NC; White, CG | 1 |
| de Ropp, JS; La Mar, GN; Mandal, PK | 1 |
| Becucci, M; Feis, A; Indiani, C; Marzocchi, MP; Smulevich, G | 1 |
| Howes, BD; Smith, AT; Smulevich, G; Veitch, NC; White, CG | 1 |
| Aitken, SM; English, AM; Percival, MD; Turnbull, JL | 1 |
| Fidy, J; Kaposi, AD; Stavrov, SS; Vanderkooi, JM; Wright, WW | 1 |
| Fidy, J; Heremans, K; Meersman, F; Smeller, L | 1 |
| Khajehpour, M; Troxler, T; Vanderkooi, JM | 1 |
| Chouchane, S; Girotto, S; Kapetanaki, S; Magliozzo, RS; Schelvis, JP; Yu, S | 1 |
| Dalosto, SD; Kaposi, AD; Prabhu, NV; Sharp, KA; Stavrov, SS; Vanderkooi, JM; Wright, WW | 1 |
| Khajehpour, M; Prabhu, NV; Rietveld, I; Sharp, KA; Vanderkooi, JM; Vinogradov, S | 1 |
| Gabdoulline, RR; Hallingbäck, HR; Wade, RC | 1 |
| Adamczyk, K; Greetham, GM; Hithell, G; Hunt, NT; Parker, AW; Shaw, DJ; Simpson, N; Towrie, M | 1 |
17 other study(ies) available for heme and benzohydroxamic acid
| Article | Year |
|---|---|
Proton nuclear Overhauser effect study of the heme active site structure of Coprinus macrorhizus peroxidase.
Topics: Binding Sites; Chemical Phenomena; Chemistry, Physical; Coprinus; Cytochrome-c Peroxidase; Heme; Histidine; Horseradish Peroxidase; Hydroxamic Acids; Magnetic Resonance Spectroscopy; Peroxidase | 1992 |
Structural studies by proton-NMR spectroscopy of plant horseradish peroxidase C, the wild-type recombinant protein from Escherichia coli and two protein variants, Phe41----Val and Arg38----Lys.
Topics: Arginine; Cyanides; Heme; Horseradish Peroxidase; Hydroxamic Acids; Isoenzymes; Lysine; Magnetic Resonance Spectroscopy; Phenylalanine; Protein Conformation; Recombinant Proteins; Structure-Activity Relationship; Valine | 1992 |
Measurement of the spin concentration of metalloprotein samples from saturation-magnetization data with particular reference to cytochrome c oxidase.
Topics: Animals; Cattle; Copper; Cytochrome c Group; Dithionite; Edetic Acid; Electron Spin Resonance Spectroscopy; Electron Transport Complex IV; Heme; Horseradish Peroxidase; Hydroxamic Acids; Magnetics; Metalloproteins | 1995 |
Probing the aromatic-donor-binding site of horseradish peroxidase using site-directed mutagenesis and the suicide substrate phenylhydrazine.
Topics: Binding Sites; Coprinus; Heme; Horseradish Peroxidase; Hydroxamic Acids; Mutagenesis, Site-Directed; Phenylhydrazines; Protein Structure, Tertiary | 1996 |
Identification of a critical phenylalanine residue in horseradish peroxidase, Phe179, by site-directed mutagenesis and 1H-NMR: implications for complex formation with aromatic donor molecules.
Topics: Benzoates; Benzoic Acid; Cyanides; Heme; Horseradish Peroxidase; Hydrogen-Ion Concentration; Hydroxamic Acids; Isoenzymes; Mutagenesis, Site-Directed; Mutation; Nuclear Magnetic Resonance, Biomolecular; Phenylalanine; Protons; Recombinant Proteins; Terminology as Topic | 1997 |
Solution 1H NMR investigation of the heme cavity and substrate binding site in cyanide-inhibited horseradish peroxidase.
Topics: Benzoates; Binding Sites; Cyanides; Enzyme Inhibitors; Heme; Histidine; Horseradish Peroxidase; Hydroxamic Acids; Macromolecular Substances; Nuclear Magnetic Resonance, Biomolecular; Solutions; Substrate Specificity | 1999 |
Peroxidase-benzhydroxamic acid complexes: spectroscopic evidence that a Fe-H2O distance of 2.6 A can correspond to hexa-coordinate high-spin heme.
Topics: Coprinus; Crystallization; Heme; Horseradish Peroxidase; Hydroxamic Acids; Iron; Isoenzymes; Metmyoglobin; Peroxidase; Recombinant Proteins; Solutions; Spectrum Analysis, Raman; Temperature; Water | 1999 |
Haem-linked interactions in horseradish peroxidase revealed by spectroscopic analysis of the Phe-221-->Met mutant.
Topics: Arabidopsis; Catalysis; Heme; Horseradish Peroxidase; Hydrogen-Ion Concentration; Hydroxamic Acids; Kinetics; Ligands; Magnetic Resonance Spectroscopy; Methionine; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Phenylalanine; Plasmids; Spectrum Analysis, Raman | 2001 |
Thermodynamic analysis of the binding of aromatic hydroxamic acid analogues to ferric horseradish peroxidase.
Topics: Benzamides; Binding Sites; Buffers; Calorimetry; Heme; Horseradish Peroxidase; Hydrazines; Hydrogen-Ion Concentration; Hydroxamic Acids; Hydroxylamines; Isoenzymes; Isoniazid; Models, Chemical; Nicotinic Acids; Salicylamides; Substrate Specificity; Thermodynamics; Titrimetry | 2001 |
Influence of static and dynamic disorder on the visible and infrared absorption spectra of carbonmonoxy horseradish peroxidase.
Topics: Heme; Horseradish Peroxidase; Hydroxamic Acids; Protein Conformation; Spectrophotometry; Spectrophotometry, Infrared; Substrate Specificity; Temperature; Thermodynamics | 2001 |
High-pressure FTIR study of the stability of horseradish peroxidase. Effect of heme substitution, ligand binding, Ca++ removal, and reduction of the disulfide bonds.
Topics: Amides; Apoenzymes; Binding Sites; Calcium; Disulfides; Enzyme Stability; Heme; Horseradish Peroxidase; Hydroxamic Acids; Ligands; Metals; Oxidation-Reduction; Porphyrins; Pressure; Protein Binding; Protein Conformation; Spectroscopy, Fourier Transform Infrared | 2003 |
Effect of protein dynamics upon reactions that occur in the heme pocket of horseradish peroxidase.
Topics: Binding Sites; Deuterium; Fluorescence Resonance Energy Transfer; Heme; Horseradish Peroxidase; Hydrogen-Ion Concentration; Hydroxamic Acids; Kinetics; Mesoporphyrins; Photochemistry; Solvents; Temperature; Thermodynamics; Viscosity | 2003 |
Conformational differences in Mycobacterium tuberculosis catalase-peroxidase KatG and its S315T mutant revealed by resonance Raman spectroscopy.
Topics: Amino Acid Substitution; Bacterial Proteins; Benzoates; Binding Sites; Catalase; Drug Resistance, Microbial; Electron Spin Resonance Spectroscopy; Ferric Compounds; Ferrous Compounds; Heme; Hydroxamic Acids; Isoniazid; Mutagenesis, Site-Directed; Mutation; Mycobacterium tuberculosis; Oxidation-Reduction; Peroxidase; Peroxidases; Protein Conformation; Recombinant Proteins; Spectrum Analysis, Raman; Spin Labels | 2003 |
Solvent dependent and independent motions of CO-horseradish peroxidase examined by infrared spectroscopy and molecular dynamics calculations.
Topics: Arginine; Binding Sites; Carbon Monoxide; Heme; Histidine; Horseradish Peroxidase; Hydrogen-Ion Concentration; Hydroxamic Acids; Models, Molecular; Movement; Solvents; Spectrophotometry, Infrared; Temperature | 2003 |
Accessibility of oxygen with respect to the heme pocket in horseradish peroxidase.
Topics: Binding Sites; Diffusion; Heme; Horseradish Peroxidase; Hydroxamic Acids; Luminescent Measurements; Mesoporphyrins; Models, Molecular; Naphthalenes; Oxygen; Palladium; Protein Binding; Solvents; Spectrum Analysis; Sulfuric Acids; Viscosity | 2003 |
Comparison of the binding and reactivity of plant and mammalian peroxidases to indole derivatives by computational docking.
Topics: Animals; Binding Sites; Coumaric Acids; Heme; Horseradish Peroxidase; Hydroxamic Acids; Indoles; Kinetics; Mammals; Melatonin; Models, Molecular; Peroxidase; Peroxidases; Plants; Protein Binding; Serotonin; Static Electricity; Structure-Activity Relationship; Substrate Specificity | 2006 |
The effect on structural and solvent water molecules of substrate binding to ferric horseradish peroxidase.
Topics: Binding Sites; Deuterium Exchange Measurement; Diffusion; Heme; Horseradish Peroxidase; Hydroxamic Acids; Kinetics; Molecular Dynamics Simulation; Molecular Probes; Nitric Oxide; Protein Binding; Protein Conformation; Solvents; Spectrophotometry, Infrared; Vibration; Water | 2015 |