heme has been researched along with potassium cyanide in 47 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 19 (40.43) | 18.7374 |
| 1990's | 12 (25.53) | 18.2507 |
| 2000's | 13 (27.66) | 29.6817 |
| 2010's | 3 (6.38) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Durham, DR; Perry, JJ | 1 |
| Klatt, P; Mayer, B; Schmidt, K | 1 |
| Ignarro, LJ; Wood, KS | 1 |
| Mitchell, P; Rich, PR; West, IC | 1 |
| Denariaz, CM; Dunford, HB; LeGall, J; Liu, MY; Marquez, L; Payne, WJ; Van Beeumen, J | 1 |
| Davies, MJ | 1 |
| Ator, MA; David, SK; Ortiz de Montellano, PR | 1 |
| Hasumi, H; Horie, S; Takizawa, N | 1 |
| Jue, T; Kauten, RJ; La Mar, GN; Langry, KC; Leung, HK; Nagai, K; Pandey, RK; Smith, KM; Thanabal, V; Yamamoto, Y | 1 |
| Hochman, A; Shemesh, A | 1 |
| Itano, HA; Kinuta, M; Matteson, JL | 1 |
| Ballot, B; Ignarro, LJ; Wolin, MS; Wood, KS | 1 |
| Hakim, J; Järvisalo, J; Torres, M | 1 |
| Cantoni, L; De Matteis, F; Gibbs, AH | 1 |
| Cammack, R; Cole, JA; Cornish-Bowden, A; Jackson, RH | 1 |
| Azzi, A; Corbley, MJ | 1 |
| Hjortsberg, K; Ohlsson, PI; Paul, KG; Smith, ML | 1 |
| Ahmed, AE; Farooqui, MY | 1 |
| Coon, MJ; White, RE | 1 |
| Alge, D; Fromwald, S; Mayer, B; Peschek, GA | 1 |
| Amada, F; Fukuyama, K; Kubota, T; Kunishima, N; Matsubara, H | 1 |
| Iwamoto, Y; Kido, R; Lee, IS; Tsubaki, M | 1 |
| Burkhalter, RS; Carraway, AD; Peterson, J; Timkovich, R | 1 |
| Arutjunjan, AM; Gennis, R; Konstantinov, AA; Krasnoselskaya, I; Smirnova, I | 1 |
| Ikebukuro, K; Karube, I; Nakanishi, K | 1 |
| Contreras, ML; Dávila, JR; Del Arenal, IP; Escamilla, JE; Lledías, F; Rangel, P; Svlateorova, BB | 1 |
| Butler, CS; Moody, AJ; Rich, PR; Thomson, AJ; Watmough, NJ | 1 |
| Liao, GL; Palmer, G | 1 |
| Beljanovich, LM; Konev, SV; Rudenok, AN | 1 |
| Aguilar, GR; Baca, BE; Contreras-Zentella, M; Escamilla, JE; Flores-Encarnación, M; Soto-Urzua, L | 1 |
| Chen, YR; Deterding, LJ; Mason, RP; Tomer, KB | 1 |
| Gladwin, MT; Nichols, JS; Ognibene, FP; Pannell, LK; Pease-Fye, ME; Schechter, AN; Shelhamer, JH | 1 |
| Hajdu, J; Sjögren, T | 1 |
| Hori, H | 1 |
| Wang, ZB; Xu, JX; Zhao, Y | 1 |
| Bominaar, EL; Hill, BC; Pearce, LL; Peterson, J | 1 |
| Goodwin, DC; Hertwig, KM; Roberts, JK; Thomas, R; Varnado, CL | 1 |
| Field, SJ; Grönberg, KL; Richardson, DJ; Thomson, AJ; Watmough, NJ | 1 |
| Falzone, CJ; Lecomte, JT; Nothnagel, HJ; Vu, BC; Vuletich, DA | 1 |
| Cheesman, MR; Ferguson, SJ; Gordon, EH; Zajicek, RS | 1 |
| Jiang, E; Lohman, J; Malavalli, A; Minn, C; Samaja, M; Vandegriff, KD; Winslow, RM; Young, MA | 1 |
| Arciero, DM; Chen, Y; Hooper, AB; Liang, Q; Timkovich, R | 1 |
| Kobayashi, K; Mogi, T; Tagawa, S | 1 |
| Davis, MF; de Serrano, V; Decatur, SM; Franzen, S; Gracz, H; Somasundaram, A; Vendeix, FA | 1 |
| Fujita, T; Inagi, R; Kawada, N; Mimura, I; Nangaku, M; Nishi, H; Yoshizato, K | 1 |
| Kukino, K; Nose, A; Sawai, H; Shiro, Y; Tsujino, H; Uno, T; Yamashita, T | 1 |
| Bennett, B; Elliott, SJ; Judd, ET; Love, D; Pacheco, AA; Stein, N | 1 |
47 other study(ies) available for heme and potassium cyanide
| Article | Year |
|---|---|
Amine dehydrogenase of Pseudomonas putida: properties of the heme-prosthetic group.
Topics: Binding, Competitive; Cuprizone; Heme; Oxidoreductases Acting on CH-NH Group Donors; Potassium Cyanide; Pseudomonas; Semicarbazides; Spectrum Analysis | 1978 |
Brain nitric oxide synthase is a haemoprotein.
Topics: Amino Acid Oxidoreductases; Animals; Brain; Carbon Monoxide; Citrulline; Heme; Miconazole; Nitric Oxide; Nitric Oxide Synthase; Potassium Cyanide; Spectrophotometry; Swine | 1992 |
Hepatic cyclic GMP formation is regulated by similar factors that modulate activation of purified hepatic soluble guanylate cyclase.
Topics: 1-Methyl-3-isobutylxanthine; Acetaminophen; Acetylcysteine; Animals; Cyclic AMP; Cyclic GMP; Guanylate Cyclase; Heme; Liver; Methylnitronitrosoguanidine; Mice; Nitroglycerin; Penicillamine; Phenobarbital; Phenylhydrazines; Potassium Cyanide; Probenecid; Protoporphyrins; Purinones; S-Nitroso-N-Acetylpenicillamine | 1987 |
The location of CuA in mammalian cytochrome c oxidase.
Topics: Adenosine Triphosphate; Animals; Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone; Cattle; Copper; Cytochrome c Group; Electron Transport Complex IV; Heme; Hydrogen-Ion Concentration; Intracellular Membranes; Ion Channels; Membrane Potentials; Mitochondria, Heart; Mitochondria, Liver; Oxidation-Reduction; Potassium Cyanide; Protons; Rats; Spectrophotometry | 1988 |
Cytochrome c peroxidase activity of a protease-modified form of cytochrome c-552 from the denitrifying bacterium Pseudomonas perfectomarina.
Topics: Amino Acid Sequence; Ascorbic Acid; Binding Sites; Cytochrome c Group; Cytochrome-c Peroxidase; Dithionite; Electron Spin Resonance Spectroscopy; Heme; Hydrolysis; Molecular Sequence Data; Oxidation-Reduction; Peptide Fragments; Peroxidases; Potassium Cyanide; Pseudomonas; Spectrophotometry; Trypsin | 1989 |
Direct detection of peroxyl radicals formed in the reactions of metmyoglobin and methaemoglobin with t-butyl hydroperoxide.
Topics: Chemical Phenomena; Chemistry; Electron Spin Resonance Spectroscopy; Heme; Hemeproteins; Methemoglobin; Metmyoglobin; Peroxides; Potassium Cyanide; tert-Butylhydroperoxide | 1989 |
Stabilized isoporphyrin intermediates in the inactivation of horseradish peroxidase by alkylhydrazines.
Topics: Alkylation; Catalysis; Enzyme Activation; Enzyme Stability; Heme; Horseradish Peroxidase; Hydrazines; Hydrogen Peroxide; Hydrogen-Ion Concentration; Isomerism; Peroxidases; Porphyrins; Potassium Cyanide; Spectrophotometry | 1989 |
Heme-linked spectral changes of the protein moiety of hemoproteins in the near ultraviolet region.
Topics: Animals; Catalase; Cattle; Cytochrome P-450 Enzyme System; Electron Transport Complex IV; Ferric Compounds; Heme; Hemeproteins; Hemoglobins; Horseradish Peroxidase; Humans; Lactoperoxidase; Methemoglobin; Muramidase; Nitrite Reductases; Oxidation-Reduction; Potassium Cyanide; Spectrophotometry; Spectrophotometry, Ultraviolet; Swine | 1985 |
1H-NMR heme resonance assignments by selective deuteration in low-spin complexes of ferric hemoglobin A.
Topics: Azides; Deuterium; Heme; Hemoglobin A; Humans; Hydrogen; Macromolecular Substances; Magnetic Resonance Spectroscopy; Potassium Cyanide; Protein Conformation; Sodium Azide | 1988 |
Purification and characterization of a catalase-peroxidase from the photosynthetic bacterium Rhodopseudomonas capsulata.
Topics: Azides; Catalase; Heme; Hydrogen Peroxide; Hydroxylamine; Hydroxylamines; Kinetics; Macromolecular Substances; Molecular Weight; Peroxidases; Potassium Cyanide; Protein Binding; Rhodopseudomonas; Sodium Azide; Spectrophotometry; Thermodynamics | 1987 |
Formation of aryl and aryldiazenyl complexes in reactions of arylhydrazines and aryldiazenes with a synthetic model compound of haemoprotein.
Topics: Carbon Monoxide; Chemical Phenomena; Chemistry; Chlorides; Heme; Imines; Macromolecular Substances; Models, Chemical; Oxygen; Phenylhydrazines; Potassium Cyanide | 1986 |
Guanylate cyclase from bovine lung. Evidence that enzyme activation by phenylhydrazine is mediated by iron-phenyl hemoprotein complexes.
Topics: Animals; Cattle; Enzyme Activation; Flavin Mononucleotide; Guanylate Cyclase; Heme; Hemeproteins; Iron; Kinetics; Lung; Molecular Weight; Nitric Oxide; Phenylhydrazines; Potassium Cyanide; Protein Binding | 1984 |
Effect of carbon disulfide on superoxide anion production by rat liver microsomes.
Topics: Aniline Compounds; Animals; Carbon Disulfide; Cytochrome c Group; Heme; Male; Microsomes, Liver; NAD; NADP; Oxygen; Phenobarbital; Potassium Cyanide; Rats; Superoxides | 1981 |
Loss of haem and haemoproteins during the generation of superoxide anion and hydrogen peroxide: a pathway not involving production of carbon monoxide.
Topics: Animals; Anions; Azides; Bile Pigments; Carbon Monoxide; Erythrocytes; Fumarates; Heme; Hemeproteins; Horses; Hydrogen Peroxide; Oxygen; Potassium Cyanide; Sodium Azide; Superoxides; Xanthine Oxidase | 1981 |
Electron-spin-resonance studies of the NADH-dependent nitrite reductase from Escherichia coli K12.
Topics: Electron Spin Resonance Spectroscopy; Escherichia coli; Heme; Iron; NADH, NADPH Oxidoreductases; Nitrite Reductase (NAD(P)H); Nitrite Reductases; Oxidation-Reduction; Potassium Cyanide; Sulfur; Thiosulfates | 1982 |
Resolution of bovine heart cytochrome c oxidase into smaller complexes by controlled subunit denaturation.
Topics: Animals; Carbon Monoxide; Catalysis; Cattle; Chemical Phenomena; Chemistry; Electron Transport Complex IV; Heme; Myocardium; Oxidation-Reduction; Potassium Cyanide; Protein Denaturation | 1984 |
The mechanism of spontaneous heme release from horseradish peroxidase isoenzyme A2.
Topics: Animals; Apoproteins; Chemical Phenomena; Chemistry; Circular Dichroism; Heme; Horseradish Peroxidase; Humans; Hydrogen-Ion Concentration; Isoenzymes; Kinetics; Myoglobin; Peroxidases; Potassium Cyanide; Temperature | 1983 |
Molecular interaction of acrylonitrile and potassium cyanide with rat blood.
Topics: Acrylonitrile; Administration, Oral; Animals; Cyanides; Erythrocytes; Heme; Hemoglobins; Male; Membrane Proteins; Nitriles; Potassium Cyanide; Rats; Rats, Inbred Strains; Time Factors | 1982 |
Heme ligand replacement reactions of cytochrome P-450. Characterization of the bonding atom of the axial ligand trans to thiolate as oxygen.
Topics: Animals; Anions; Cytochrome P-450 Enzyme System; Heme; Microsomes, Liver; Phenobarbital; Potassium Cyanide; Protein Binding; Rabbits; Spectrophotometry | 1982 |
Transient accumulation of heme O (cytochrome o) in the cytoplasmic membrane of semi-anaerobic Anacystis nidulans. Evidence for oxygenase-catalyzed heme O/A transformation.
Topics: Anaerobiosis; Cell Membrane; Chromatography, High Pressure Liquid; Cyanobacteria; Cytochrome b Group; Cytochrome c Group; Cytochromes; Diuron; Electron Transport; Escherichia coli Proteins; Heme; Immunoblotting; Kinetics; Membrane Proteins; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Oxygen Consumption; Potassium Cyanide | 1995 |
Crystal structures of cyanide- and triiodide-bound forms of Arthromyces ramosus peroxidase at different pH values. Perturbations of active site residues and their implication in enzyme catalysis.
Topics: Amino Acid Sequence; Arginine; Binding Sites; Computer Graphics; Crystallography, X-Ray; Fourier Analysis; Heme; Histidine; Hydrogen-Ion Concentration; Iodides; Mitosporic Fungi; Models, Molecular; Periodic Acid; Peroxidases; Potassium Compounds; Potassium Cyanide | 1995 |
Tryptophan 2,3-dioxygenase in Saccharomyces cerevisiae.
Topics: Azides; Binding Sites; Chromatography, Liquid; Electrophoresis, Gel, Two-Dimensional; Fungal Proteins; Heme; Hydrogen-Ion Concentration; Isoelectric Point; Kynurenine; Potassium Cyanide; Saccharomyces cerevisiae; Sodium Azide; Substrate Specificity; Tryptophan; Tryptophan Oxygenase | 1995 |
Characterization of heme c peptides by mass spectrometry.
Topics: Amino Acid Sequence; Amino Acids; Binding Sites; Cytochrome c Group; Heme; Hydrolysis; Molecular Sequence Data; Potassium Cyanide; Spectrometry, Mass, Fast Atom Bombardment | 1993 |
Cyanide-reactive sites in cytochrome bd complex from E. coli.
Topics: Binding Sites; Circular Dichroism; Cytochrome b Group; Cytochromes; Electron Transport Chain Complex Proteins; Escherichia coli; Escherichia coli Proteins; Heme; Magnetics; Oxidoreductases; Potassium Cyanide | 1993 |
Determination of cyanide using a microbial sensor.
Topics: Cyanides; Cytochrome a Group; Electrodes; Electron Transport; Electron Transport Complex IV; Glucose; Heme; Hydrogen-Ion Concentration; Potassium Cyanide; Saccharomyces cerevisiae; Sodium Cyanide; Solutions | 1996 |
Haem O and a putative cytochrome bo in a mutant of Bacillus cereus impaired in the synthesis of haem A.
Topics: Bacillus cereus; Cytochrome b Group; Cytochrome c Group; Cytochromes; Escherichia coli Proteins; Heme; Molecular Weight; Multienzyme Complexes; Mutation; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Potassium Cyanide; Spores, Bacterial | 1997 |
The reaction of halides with pulsed cytochrome bo from Escherichia coli.
Topics: Binding Sites; Bromides; Chlorides; Cytochrome b Group; Cytochromes; Electron Spin Resonance Spectroscopy; Escherichia coli; Escherichia coli Proteins; Heme; Hydrogen-Ion Concentration; Iodides; Kinetics; Potassium Cyanide; Spectrophotometry, Infrared | 1998 |
Diazene--a not so innocent ligand for the binuclear center of cytochrome c oxidase.
Topics: Animals; Cattle; Electron Spin Resonance Spectroscopy; Electron Transport Complex IV; Heme; Horseradish Peroxidase; Hydrazines; Imides; Ligands; Models, Molecular; Myoglobin; Oxidation-Reduction; Oxygen; Potassium Cyanide; Spectrophotometry | 1998 |
Photoreactivation of the cytochrome oxidase complex with cyanide: the reaction of heme a3 photoreduction.
Topics: Animals; Cattle; Cytochrome c Group; Electron Transport; Electron Transport Complex IV; Heme; Mitochondria, Liver; Mitochondria, Muscle; Myocardium; Oxidation-Reduction; Oxygen Consumption; Photochemistry; Potassium Cyanide; Rats | 1998 |
The respiratory system and diazotrophic activity of Acetobacter diazotrophicus PAL5.
Topics: Acetobacter; Culture Media; Cytochromes; Electron Transport; Heme; Nitrogen Fixation; Oxidation-Reduction; Oxygen Consumption; Potassium Cyanide; Quaternary Ammonium Compounds; Temperature | 1999 |
Nature of the inhibition of horseradish peroxidase and mitochondrial cytochrome c oxidase by cyanyl radical.
Topics: Apoenzymes; Catalysis; Chromatography, High Pressure Liquid; Cyanides; Cyclic N-Oxides; Electron Spin Resonance Spectroscopy; Electron Transport Complex IV; Ethylmaleimide; Guaiacol; Heme; Holoenzymes; Horseradish Peroxidase; Hydrogen Peroxide; Magnetic Resonance Spectroscopy; Mitochondria; Models, Chemical; Molecular Weight; Oxidative Stress; Potassium Cyanide; Protons; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spin Trapping | 2000 |
Relative role of heme nitrosylation and beta-cysteine 93 nitrosation in the transport and metabolism of nitric oxide by hemoglobin in the human circulation.
Topics: Administration, Inhalation; Cysteine; Heme; Hemoglobins; Humans; Kinetics; Luminescent Measurements; Nitrates; Nitric Oxide; Nitrites; Nitroso Compounds; Ozone; Potassium Cyanide; Reproducibility of Results; Sensitivity and Specificity | 2000 |
The Structure of an alternative form of Paracoccus pantotrophus cytochrome cd(1) nitrite reductase.
Topics: Binding Sites; Crystallography, X-Ray; Cytochrome c Group; Cytochromes; Freezing; Heme; Hydrogen Bonding; Models, Molecular; Nitrite Reductases; Oxidation-Reduction; Paracoccus; Potassium Cyanide; Protein Conformation; Protein Structure, Secondary; Spectrophotometry; Synchrotrons | 2001 |
Analysis of the principal g-tensors in single crystals of ferrimyoglobin complexes.
Topics: Animals; Electron Spin Resonance Spectroscopy; Heme; Histidine; Imidazoles; Metmyoglobin; Models, Molecular; Muscle, Skeletal; Potassium Cyanide; Sodium Azide; Thiocyanates; Whales | 1971 |
Effect of cytochrome c on the generation and elimination of O2*- and H2O2 in mitochondria.
Topics: Animals; Apoptosis; Cattle; Cytochrome c Group; Dose-Response Relationship, Drug; Down-Regulation; Electron Transport; Electrons; Heme; Hydrogen Peroxide; Kinetics; Luminescent Measurements; Myocardium; Oxidation-Reduction; Potassium Cyanide; Reactive Oxygen Species; Spectrophotometry; Time Factors | 2003 |
Reversal of cyanide inhibition of cytochrome c oxidase by the auxiliary substrate nitric oxide: an endogenous antidote to cyanide poisoning?
Topics: Animals; Brain; Catalysis; Cattle; Copper; Cyanides; Cytochromes c; Electron Spin Resonance Spectroscopy; Electron Transport Complex IV; Electrons; Heme; Histidine; Iron; Kinetics; Magnetics; Mitochondria; Models, Chemical; Myocardium; Nitric Oxide; Oxygen; Potassium Cyanide; Spectrophotometry | 2003 |
Properties of a novel periplasmic catalase-peroxidase from Escherichia coli O157:H7.
Topics: Bacterial Proteins; Cloning, Molecular; Escherichia coli O157; Ferric Compounds; Ferrous Compounds; Heme; Hydrogen Peroxide; Isoenzymes; Kinetics; Peracetic Acid; Peroxidases; Potassium Cyanide; Recombinant Proteins; Spectrophotometry, Ultraviolet; Virulence | 2004 |
Redox-dependent open and closed forms of the active site of the bacterial respiratory nitric-oxide reductase revealed by cyanide binding studies.
Topics: Bacteria; Binding Sites; Catalysis; Cyanides; Dose-Response Relationship, Drug; Electrons; Heme; Iron; Kinetics; Ligands; Nitric Oxide; Oxidation-Reduction; Oxidoreductases; Oxygen; Oxygen Consumption; Paracoccus denitrificans; Potassium Cyanide; Protein Binding; Time Factors; Ultraviolet Rays | 2004 |
Cyanide binding to hexacoordinate cyanobacterial hemoglobins: hydrogen-bonding network and heme pocket rearrangement in ferric H117A Synechocystis hemoglobin.
Topics: Alanine; Bacterial Proteins; Binding Sites; Cyanobacteria; Heme; Hemeproteins; Hemoglobins; Histidine; Hot Temperature; Hydrogen Bonding; Imidazoles; Iron; Mutagenesis, Site-Directed; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular; Potassium Cyanide; Protein Binding; Protein Denaturation; Recombinant Proteins; Truncated Hemoglobins | 2004 |
Y25S variant of Paracoccus pantotrophus cytochrome cd1 provides insight into anion binding by d1 heme and a rare example of a critical difference between solution and crystal structures.
Topics: Anions; Binding Sites; Crystallography, X-Ray; Cytochrome c Group; Cytochromes; Electron Spin Resonance Spectroscopy; Escherichia coli; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Ligands; Mutation; Nitric Oxide; Nitrite Reductases; Nitrites; Oxygen; Paracoccus pantotrophus; Potassium Cyanide; Protein Binding; Spectrophotometry; Temperature; Tyrosine; Ultraviolet Rays | 2005 |
Oxidation and haem loss kinetics of poly(ethylene glycol)-conjugated haemoglobin (MP4): dissociation between in vitro and in vivo oxidation rates.
Topics: Animals; Ascorbic Acid; Blood Substitutes; Catalase; Heme; Hemoglobins; Humans; Male; Maleimides; Methemoglobin; Oxidation-Reduction; Polyethylene Glycols; Potassium Cyanide; Rats; Rats, Sprague-Dawley; Reactive Oxygen Species; Xanthine; Xanthine Oxidase | 2006 |
Heme crevice disorder after sixth ligand displacement in the cytochrome c-551 family.
Topics: Bacterial Proteins; Cytochrome c Group; Electron Spin Resonance Spectroscopy; Heme; Hydrogen-Ion Concentration; Ligands; Methionine; Nitrosomonas; Nuclear Magnetic Resonance, Biomolecular; Potassium Cyanide; Protein Conformation; Protein Isoforms; Pseudomonas | 2007 |
Intramolecular electron transfer processes in Cu(B)-deficient cytochrome bo studied by pulse radiolysis.
Topics: Alanine; Amino Acid Substitution; Copper; Cytochrome b Group; Electron Transport; Escherichia coli; Escherichia coli Proteins; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Mutation; Oxidation-Reduction; Potassium Cyanide; Potentiometry; Pulse Radiolysis | 2009 |
Different modes of binding of mono-, di-, and trihalogenated phenols to the hemoglobin dehaloperoxidase from Amphitrite ornata.
Topics: Animals; Binding Sites; Catalysis; Catalytic Domain; Heme; Hemoglobins; Hydrocarbons, Halogenated; Molecular Conformation; Nuclear Magnetic Resonance, Biomolecular; Peroxidases; Phenols; Polychaeta; Potassium Cyanide; Protein Binding; Protein Conformation; Recombinant Proteins; Substrate Specificity | 2009 |
Cytoglobin, a novel member of the globin family, protects kidney fibroblasts against oxidative stress under ischemic conditions.
Topics: Amino Acid Sequence; Animals; Base Sequence; Cytoglobin; Fibroblasts; Gene Knockdown Techniques; Globins; Heme; Ischemia; Kidney; Molecular Sequence Data; Oxidative Stress; Potassium Cyanide; Rats; Rats, Transgenic; Reperfusion Injury | 2011 |
Disulfide bonds regulate binding of exogenous ligand to human cytoglobin.
Topics: Amino Acid Substitution; Carbon Monoxide; Cystine; Cytoglobin; Globins; Heme; Humans; Kinetics; Ligands; Mutagenesis, Site-Directed; Oxidation-Reduction; Potassium Cyanide; Protein Binding; Protein Multimerization; Spectrum Analysis, Raman | 2014 |
Correlations between the Electronic Properties of Shewanella oneidensis Cytochrome c Nitrite Reductase (ccNiR) and Its Structure: Effects of Heme Oxidation State and Active Site Ligation.
Topics: Amino Acid Substitution; Bacterial Proteins; Catalytic Domain; Cytochromes a1; Cytochromes c1; Electron Spin Resonance Spectroscopy; Enzyme Inhibitors; Heme; Ligands; Models, Molecular; Molecular Conformation; Mutagenesis, Site-Directed; Mutant Proteins; Nitrate Reductases; Oxidation-Reduction; Potassium Cyanide; Protein Conformation; Recombinant Proteins; Shewanella; Sodium Nitrite; Spectrophotometry; Titrimetry | 2015 |