dithionite and heme
dithionite has been researched along with heme in 82 studies
Research
Studies (82)
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 31 (37.80) | 18.7374 |
| 1990's | 22 (26.83) | 18.2507 |
| 2000's | 20 (24.39) | 29.6817 |
| 2010's | 9 (10.98) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
Authors
| Authors | Studies |
|---|---|
| Aparicio, PJ; Knaff, DB; Malkin, R | 1 |
| Iizuka, T; Orii, Y; Yoshida, S | 1 |
| Kim, IC | 1 |
| Mincey, T; Traylor, TG | 1 |
| DeFilippi, LJ; Hultquist, DE; Toler, LS | 1 |
| Brittain, T; Greenwood, C; Springall, JP; Thomson, AJ | 1 |
| Coin, JT; Olson, JS | 1 |
| Orii, Y; Shimada, H | 1 |
| Liem, HH; Morgan, WT; Muller-Ebergard, U; Sutor, RP | 1 |
| Horie, S; Nakamura, S; Watanabe, T | 1 |
| Andreesen, JR; Gottwald, M; LeGall, J; Ljungdahl, LG | 1 |
| Gibson, QH; Moore, EG | 1 |
| Cooper, CE; Salerno, JC | 1 |
| Anraku, Y; Gennis, RB; Minagawa, J; Mogi, T | 1 |
| Calhoun, MW; Gennis, RB; Ingledew, WJ; Lemieux, LJ; Thomas, JW | 1 |
| Puustinen, A | 1 |
| Puustinen, A; Wikström, M | 1 |
| Droupadi, PR; Herzfeld, J; Seidel, NE; Taylor, MP; Wang, NE | 1 |
| Güner, S; Hobbs, DD; Knaff, DB; Kriauciunas, A; Ondrias, MR | 1 |
| Blackmore, RS; Gadsby, PM; Greenwood, C; Thomson, AJ | 1 |
| Blackmore, RS; Brittain, T; Gadsby, PM; Greenwood, C; Thomson, AJ | 1 |
| Denariaz, CM; Dunford, HB; LeGall, J; Liu, MY; Marquez, L; Payne, WJ; Van Beeumen, J | 1 |
| Neupert, W; Nicholson, DW | 1 |
| Muhoberac, BB; Steup, MB | 1 |
| Arif Kazmi, S; Mills, MA; Pitluk, ZW; Scott, RA | 1 |
| DerVartanian, DV; Le Gall, J; Liu, MC; Liu, MY; Payne, WJ; Peck, HD | 1 |
| Gibbs, EJ; Hashim, M; Kurokawa, K; Mauk, AG; Muller-Eberhard, U; Pasternack, RF; Reid, LS; Wong, NM | 1 |
| Coon, MJ; van der Hoeven, TA | 1 |
| Bucci, E | 1 |
| Odajima, T | 1 |
| Hildebrandt, V; Nicholls, P; Wrigglesworth, JM | 1 |
| Barber, D; Greenwood, C; Johnson, MK; Thomson, AJ; Walsh, TA | 1 |
| Schilder, LT; Tervoort, MJ; Van Gelder, BF | 1 |
| Ho, PS; Hoffman, BM; Kang, CH; Margoliash, E | 1 |
| Balny, C; Hooper, AB; Tran, VM | 1 |
| Kulmacz, RJ; Lands, WE; Titus, BG | 1 |
| Lambeth, JD; Pember, SO | 1 |
| Morita, S; Takaichi, S | 1 |
| Bumpus, JA; Dus, KM; Hanukoglu, I; Jefcoate, CR; Spitsberg, V | 1 |
| Peck, HD; Steenkamp, DJ | 1 |
| Gennis, RB; Georgiou, C; Ghaim, JB; Kaysser, TM | 1 |
| Day, EP; Pearce, LL; Peterson, J; Wilson, MT | 1 |
| Fu, R; Voordouw, G; Wall, JD | 1 |
| Albanese, J; Hill, BC; Vo, L | 1 |
| Chottard, G; Gaspard, S; Mahy, JP; Mansuy, D | 1 |
| Doussière, J; Gaillard, J; Vignais, PV | 2 |
| Blanke, SR; Dawson, JH; Hager, LP; Hoa, GH; Martinis, SA; Rux, JJ; Sligar, SG | 1 |
| Desbois, A; Escriou, V; Laporte, F; Vignais, PV | 1 |
| Azarkina, N; Borisov, V; Konstantinov, AA | 1 |
| Boyington, JC; Kulansky, R; Malech, HL; Rafferty, SP; Sun, PD | 1 |
| Ikeda, T; Kano, K; Kawaguchi, K; Takagi, K; Torimura, M | 1 |
| Fromwald, S; Lübben, M; Peschek, GA; Wastyn, M; Zoder, R | 1 |
| Ichihashi, D; Ichise, N; Istokovics, A; Iwata, H; Kawasaki, K; Matsuyama, H; Okuyama, H; Yumoto, I | 1 |
| Aki, M; Jin, Y; Kitagawa, T; Li, R; Nagai, M; Nagatomo, S; Sakai, H | 1 |
| Lukat-Rodgers, GS; Rodgers, KR; Tang, L | 1 |
| Dunham, WR; Hollenberg, PF; Kent, UM; Moon, N; Roberts-Kirchhoff, ES | 1 |
| Desbois, A; Gomez de Gracia, A; Le Moigne, C; Picaud, T | 1 |
| Hirose, K; Iino, M; Namiki, S | 1 |
| Garg, SK; Tekwani, BL; Tripathi, AK | 1 |
| Harada, S; Hayashi, S; Noguchi, M; Omata, Y; Palmer, G; Sakamoto, H | 1 |
| Baymann, F; Dolla, A; Durand, MC; Lexa, D; Lojou, E; Schoepp-Cothenet, B; Schütz, M; Stetter, KO; Tron, P; Woodstra, M | 1 |
| Allen, JW; Barker, PD; Ferguson, SJ | 1 |
| Edmondson, DE; Hurshman, AR; Krebs, C; Marletta, MA | 1 |
| Buc, J; Giordani, R | 1 |
| Burstyn, JN; Clark, RW; Kraus, JP; Lukat-Rodgers, GS; Oliveriusová, J; Parks, RB; Pazicni, S; Rees, KA; Rodgers, KR | 1 |
| Belevich, I; Borisov, VB; Gennis, RB; Konstantinov, AA; Verkhovsky, MI; Yang, K; Zhang, J | 1 |
| Aoyama, Y; Chung, SK; Kudo, M; Nitahara, Y; Ohi, M; Yoshida, Y | 1 |
| Burstyn, JN; Cherney, MM; Kraus, JP; Lukat-Rodgers, GS; Oliveriusová, J; Pazicni, S; Rodgers, KR | 1 |
| Corcelli, A; Lobasso, S; Palese, LL; Papa, S; Saponetti, MS | 1 |
| Escalante-Semerena, JC; Lewis, JA | 1 |
| Basu, S; Gladwin, MT; Grubina, R; Kim-Shapiro, DB; Tiso, M | 1 |
| Bröcker, MJ; Ganskow, S; Heathcote, P; Heinz, DW; Jahn, D; Moser, J; Schubert, WD; Virus, S | 1 |
| Asard, H; Bérczi, A; Desmet, F; Van Doorslaer, S | 1 |
| Makino, M; Sawai, H; Shiro, Y; Sugimoto, H | 1 |
| Egawa, T; Gerfen, GJ; Rousseau, DL; Shinzawa-Itoh, K; Yeh, SR; Yoshikawa, S; Yu, MA | 1 |
| He, C; Knipp, M; Taing, JJ | 1 |
| Borges, N; Catarino, T; Cepeda, AP; Quintas, PO; Turner, DL | 1 |
| Chauvet, A; Cramer, WA; Hasan, SS; Savikhin, S; Stadnytskyi, V; Zakharov, SD | 1 |
| Ascenzi, P; Coletta, M; Fiocchetti, M; Santucci, R; Sbardella, D | 1 |
| Azarkina, N; Dyuba, AV; Konstantinov, AA; Vygodina, T | 1 |
| Billig, S; Birkemeyer, C; Boss, L; Layer, G; Oehme, R | 1 |
Other Studies
82 other study(ies) available for dithionite and heme
| Article | Year |
|---|---|
The role of an iron-sulfur center and siroheme in spinach nitrite reductase.
Topics: Chromatography, Gel; Cyanides; Dithionite; Electron Spin Resonance Spectroscopy; Electron Transport; Heme; Iron; Nitrate Reductases; Nitrates; Plants; Porphyrins; Spectrum Analysis; Structure-Activity Relationship; Sulfur | 1975 |
Heme a and copper environments in cytochrome oxidase.
Topics: Animals; Binding Sites; Calorimetry; Carbon Monoxide; Cattle; Chloromercuribenzoates; Copper; Dithionite; Electron Transport Complex IV; Heme; Kinetics; Light; Myocardium; Oxidation-Reduction; Protein Binding; Protein Conformation; Spectrophotometry; Thermodynamics | 1976 |
Isolation and partial characterization of a new soluble b-type cytochrome (b9) from rat liver.
Topics: Animals; Cytochrome b Group; Cytochromes; Dithionite; Erythrocytes; Heme; Humans; Kidney; Liver; Macromolecular Substances; Molecular Weight; Organ Specificity; Oxidation-Reduction; Rats; Species Specificity; Spectrophotometry; Swine | 1979 |
Mercaptide chelated protoheme: a model compound for cytochrome P-450.
Topics: Carbon Monoxide; Chemical Phenomena; Chemistry; Cytochrome P-450 Enzyme System; Dimethyl Sulfoxide; Disulfides; Dithionite; Heme; Models, Biological; Spectrophotometry; Sulfhydryl Compounds | 1979 |
Reactivities of hydroxylamine and sodium bisulphite with carbonyl-containing haems and with the prosthetic groups of the erythrocyte green haemoproteins.
Topics: Animals; Cattle; Chemical Phenomena; Chemistry; Dithionite; Erythrocytes; Heme; Hemeproteins; Humans; Hydroxylamines; Oximes; Spectrophotometry; Sulfites | 1979 |
Magnetic-circular-dichroism studies of haem a and its derivatives.
Topics: Chemical Phenomena; Chemistry; Circular Dichroism; Dithionite; Heme; Oxidation-Reduction; Pyridines; Spectrophotometry, Atomic | 1978 |
The rate of oxygen uptake by human red blood cells.
Topics: Diffusion; Dithionite; Erythrocyte Membrane; Erythrocytes; Heme; Hemoglobins; Humans; Kinetics; Light; Male; Mathematics; Oxygen Consumption; Scattering, Radiation | 1979 |
Oxidation-reduction behavior of the heme c and heme d moieties of Pseudomonas aeruginosa nitrite reductase and the formation of an oxygenated intermediate at heme d1.
Topics: Ascorbic Acid; Catalase; Dithionite; Heme; NADH, NADPH Oxidoreductases; Nitrite Reductases; Oxidation-Reduction; Oxygen Consumption; Pseudomonas aeruginosa; Spectrophotometry | 1976 |
Transfer of heme from heme-albumin to hemopexin.
Topics: Apoproteins; Blood; Dithionite; Heme; Hemopexin; Humans; Serum Albumin; Temperature | 1976 |
Isolation, properties, and crystallization of an iron-chlorin protein from Aspergillus niger.
Topics: Aspergillus; Aspergillus niger; Bacterial Proteins; Crystallization; Cyanides; Dithionite; Heme; Hemeproteins; Hydroxylamines; Molecular Weight; Nitrite Reductases; Nitrites; Oxidoreductases; Paraquat; Protein Binding; Sulfites | 1976 |
Presence of cytochrome and menaquinone in Clostridium formicoaceticum and Clostridium thermoaceticum.
Topics: Bicarbonates; Cell Fractionation; Clostridium; Cytochromes; Dithionite; Formates; Fumarates; Heme; Indicators and Reagents; Vitamin K | 1975 |
Cooperativity in the dissociation of nitric oxide from hemoglobin.
Topics: Binding Sites; Dithionite; Heme; Hemoglobins; Humans; Kinetics; Myoglobin; Nitric Oxide; Protein Binding; Spectrophotometry; Time Factors | 1976 |
Characterization of a novel g' = 2.95 EPR signal from the binuclear center of mitochondrial cytochrome c oxidase.
Topics: Animals; Cattle; Dithionite; Electron Spin Resonance Spectroscopy; Electron Transport Complex IV; Heme; Microwaves; Mitochondria, Heart; Temperature | 1992 |
Identification of heme and copper ligands in subunit I of the cytochrome bo complex in Escherichia coli.
Topics: Aerobiosis; Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Copper; Dithionite; DNA, Bacterial; Electron Transport Complex IV; Escherichia coli; Genetic Complementation Test; Heme; Humans; Ligands; Macromolecular Substances; Models, Structural; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Oxidation-Reduction; Protein Conformation; Recombinant Proteins; Restriction Mapping; Sequence Homology, Nucleic Acid | 1992 |
Determination of the ligands of the low spin heme of the cytochrome o ubiquinol oxidase complex using site-directed mutagenesis.
Topics: Amino Acid Sequence; Base Sequence; Dithionite; Electron Spin Resonance Spectroscopy; Electron Transport Complex IV; Escherichia coli; Genetic Complementation Test; Genotype; Heme; Histidine; Ligands; Models, Structural; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Plasmids; Protein Conformation; Recombinant Proteins; Restriction Mapping; Thermodynamics | 1992 |
A novel type haem group of cytochrome o from Escherichia coli.
Topics: Chromatography, High Pressure Liquid; Cytochrome b Group; Cytochromes; Dithionite; Escherichia coli; Escherichia coli Proteins; Heme; Magnetic Resonance Spectroscopy; Spectrometry, Mass, Fast Atom Bombardment; Spectrophotometry, Infrared | 1992 |
The heme groups of cytochrome o from Escherichia coli.
Topics: Carbon Monoxide; Cell Membrane; Cytochrome b Group; Cytochromes; Dithionite; Escherichia coli; Escherichia coli Proteins; Heme; Oxidation-Reduction; Spectrophotometry | 1991 |
Gentle chemical deoxygenation of hemoglobin solutions.
Topics: Benzoates; Benzoic Acid; Birefringence; Catalase; Dithionite; Dithiothreitol; Edetic Acid; Heme; Hemoglobins; Horseradish Peroxidase; Humans; Methemoglobin; Oxidation-Reduction; Sulfhemoglobin; Superoxide Dismutase | 1990 |
Resonance Raman spectroscopy of cytochrome bc1 complexes from Rhodospirillum rubrum: initial characterization and reductive titrations.
Topics: Ascorbic Acid; Dithionite; Electrochemistry; Electron Transport; Electron Transport Complex III; Ferricyanides; Heme; Oxidation-Reduction; Photochemistry; Rhodospirillum rubrum; Spectrophotometry; Spectrum Analysis, Raman | 1990 |
The effect of haem ligands on the redox states of the hexa-haem nitrite reductase from Wolinella succinogenes.
Topics: Bacteroidaceae; Binding Sites; Carbon Monoxide; Circular Dichroism; Dithionite; Electron Spin Resonance Spectroscopy; Heme; Kinetics; Nitrite Reductases; Oxidation-Reduction; Sodium Cyanide; Spectrophotometry; Thermodynamics | 1990 |
Two structurally and kinetically distinct forms of Wolinella succinogenes nitrite reductase.
Topics: Bacteroidaceae; Circular Dichroism; Dithionite; Electron Spin Resonance Spectroscopy; Heme; Kinetics; Nitrite Reductases; Oxidation-Reduction; Paraquat; Spectrophotometry | 1990 |
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 |
Import of cytochrome c into mitochondria: reduction of heme, mediated by NADH and flavin nucleotides, is obligatory for its covalent linkage to apocytochrome c.
Topics: Apoproteins; Cytochrome c Group; Cytochromes c; Dithionite; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Kinetics; Lyases; Mitochondria; NAD; Oxidation-Reduction; Saccharomyces cerevisiae | 1989 |
Preparation and spectral characterization of the heme d1.apomyoglobin complex: an unusual protein environment for the substrate-binding heme of Pseudomonas cytochrome oxidase.
Topics: Apoproteins; Carbon Monoxide; Cyanides; Dithionite; Electron Spin Resonance Spectroscopy; Electron Transport Complex IV; Heme; Ligands; Myoglobin; Oxidation-Reduction; Protein Binding; Pseudomonas; Solutions; Spectrophotometry | 1989 |
Kinetics of dithionite reduction of the heme nonapeptide of cytochrome c.
Topics: Animals; Cytochrome c Group; Cytochromes c; Dithionite; Heme; Horses; Hydrogen-Ion Concentration; In Vitro Techniques; Kinetics; Myocardium; Osmolar Concentration; Oxidation-Reduction; Peptide Fragments | 1985 |
Comparative EPR studies on the nitrite reductases from Escherichia coli and Wolinella succinogenes.
Topics: Bacteroidaceae; Dithionite; Electron Spin Resonance Spectroscopy; Escherichia coli; Heme; NADH, NADPH Oxidoreductases; Nitrite Reductases; Nitrites; Oxidation-Reduction | 1987 |
Kinetics of hemoprotein reduction and interprotein heme transfer.
Topics: Dithionite; Heme; Hemeproteins; Hemopexin; Humans; Kinetics; Mathematics; Oxidation-Reduction; Protein Binding; Serum Albumin; Spectrophotometry | 1985 |
Preparation and properties of partially purified cytochrome P-450 and reduced nicotinamide adenine dinucleotide phosphate-cytochrome P-450 reductase from rabbit liver microsomes.
Topics: Animals; Binding Sites; Carbon Monoxide; Centrifugation, Density Gradient; Chromatography, DEAE-Cellulose; Chromatography, Gel; Cytochrome P-450 Enzyme System; Cytochrome Reductases; Detergents; Dithionite; Electrophoresis, Disc; Electrophoresis, Polyacrylamide Gel; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Kinetics; Male; Microsomes, Liver; Mixed Function Oxygenases; Molecular Weight; NADP; Oxidation-Reduction; Phospholipids; Polyethylene Glycols; Protein Binding; Rabbits; Solubility; Spectrophotometry; Spectrophotometry, Ultraviolet; Sulfides | 1974 |
The reversible titration of tyrosyl residues in human deoxyhemoglobin.
Topics: Acetylation; Amino Acids; Carboxyhemoglobin; Dithionite; Heme; Hemoglobins; Humans; Hydrogen-Ion Concentration; Imidazoles; Protein Binding; Protein Conformation; Spectrophotometry; Thermodynamics; Tyrosine; Ultracentrifugation | 1973 |
Myeloperoxidase of the leukocyte of normal blood. Nature of the prosthetic group of myeloperoxidase.
Topics: Animals; Benzoates; Borohydrides; Chemical Phenomena; Chemistry; Dithionite; Electron Spin Resonance Spectroscopy; Electron Transport; Heme; Iron; Leukocytes; Peroxidase; Peroxidases; Spectrophotometry; Swine | 1980 |
Orientation and reactivity of cytochrome aa3 heme groups in proteoliposomes.
Topics: Ascorbic Acid; Azides; Chemical Phenomena; Chemistry; Cyanides; Cytochrome c Group; Dithionite; Electron Transport Complex IV; Heme; Liposomes; Oxidation-Reduction; Paraquat; Tetramethylphenylenediamine | 1980 |
Studies on heme d1 extracted from Pseudomonas aeruginosa nitrite reductase.
Topics: Carbon Monoxide; Cyanides; Dithionite; Electron Spin Resonance Spectroscopy; Heme; Hydrogen-Ion Concentration; Imidazoles; Iron; NADH, NADPH Oxidoreductases; Nitric Oxide; Nitrite Reductases; Protein Binding; Pseudomonas aeruginosa; Spectrophotometry | 1981 |
The absorbance coefficient of beef heart cytochrome c1.
Topics: Animals; Cattle; Cytochrome c Group; Cytochromes; Cytochromes c1; Dithionite; Ferricyanides; Heme; Kinetics; Methylphenazonium Methosulfate; NAD; Oxidation-Reduction; Spectrophotometry | 1981 |
Control of the transfer of oxidizing equivalents between heme iron and free radical site in yeast cytochrome c peroxidase.
Topics: Cytochrome-c Peroxidase; Dithionite; Electron Spin Resonance Spectroscopy; Free Radicals; Heme; Iron; Kinetics; Oxygen Consumption; Peroxidases; Protein Binding; Saccharomyces cerevisiae; Spectrophotometry | 1983 |
Kinetics of reduction by substrate or dithionite and heme-heme electron transfer in the multiheme hydroxylamine oxidoreductase.
Topics: Anaerobiosis; Binding Sites; Dithionite; Electron Transport; Heme; Hydrazines; Hydrogen-Ion Concentration; Hydroxylamine; Hydroxylamines; Kinetics; Nitrosomonas; Oxidation-Reduction; Oxidoreductases | 1984 |
Selective destruction and removal of heme from prostaglandin H synthase.
Topics: Animals; Apoenzymes; Apoproteins; Dithionite; Heme; Male; Oxidation-Reduction; Oxygen; Prostaglandin-Endoperoxide Synthases; Seminal Vesicles; Sheep; Spectrum Analysis | 1982 |
Cytochrome P-450scc-adrenodoxin complex. Reduction properties of the substrate-associated cytochrome and relation of the reduction states of heme and iron-sulfur centers to association of the proteins.
Topics: Adrenodoxin; Animals; Cattle; Cytochrome P-450 Enzyme System; Dithionite; Heme; Hydrogen-Ion Concentration; Iron-Sulfur Proteins; Mathematics; Models, Chemical; Oxidation-Reduction | 1983 |
Procedures and conditions for application of the pyridine hemochrome method to photosynthetically grown cells of Rhodopseudomonas sphaeroides.
Topics: Dithionite; Drug Stability; Heme; Oxidation-Reduction; Photosynthesis; Pyridines; Rhodobacter sphaeroides; Solvents; Spectrophotometry | 1981 |
Adrenal mitochondrial cytochrome P-450scc. Cholesterol and adrenodoxin interactions at equilibrium and during turnover.
Topics: Adrenal Cortex; Adrenodoxin; Amino Acids; Animals; Cattle; Cholesterol; Cytochrome P-450 Enzyme System; Dithionite; Heme; Kinetics; Mitochondria; Oxidation-Reduction; Peptide Fragments; Pseudomonas; Spectrophotometry; Thermodynamics | 1981 |
The association of hydrogenase and dithionite reductase activities with the nitrite reductase of Desulfovibrio desulfuricans.
Topics: Cell Membrane; Desulfovibrio; Dithionite; Electron Transport; Heme; Hydrogen; Kinetics; Molecular Weight; NADH, NADPH Oxidoreductases; Nitrite Reductases; Oxidation-Reduction; Spectrophotometry; Sulfites | 1980 |
Methionine-393 is an axial ligand of the heme b558 component of the cytochrome bd ubiquinol oxidase from Escherichia coli.
Topics: Amino Acid Sequence; Base Sequence; Cytochrome b Group; Cytochromes; Dithionite; Electron Transport Chain Complex Proteins; Escherichia coli; Escherichia coli Proteins; Genotype; Heme; Histidine; Leucine; Ligands; Macromolecular Substances; Methionine; Molecular Sequence Data; Mutagenesis, Site-Directed; NADPH Oxidases; Oligodeoxyribonucleotides; Oxidation-Reduction; Oxidoreductases; Point Mutation; Protein Structure, Secondary; Recombinant Proteins; Restriction Mapping; Spectrophotometry | 1995 |
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 |
DcrA, a c-type heme-containing methyl-accepting protein from Desulfovibrio vulgaris Hildenborough, senses the oxygen concentration or redox potential of the environment.
Topics: Amino Acid Sequence; Antibodies, Bacterial; Bacterial Proteins; Desulfovibrio; Desulfovibrio vulgaris; Dithionite; Heme; Isotope Labeling; Membrane Proteins; Methyl-Accepting Chemotaxis Proteins; Molecular Sequence Data; Oxidation-Reduction; Oxygen; Precipitin Tests; Recombinant Fusion Proteins; Signal Transduction | 1994 |
Kinetic and ligand binding evidence for two heme A-based terminal oxidases in plasma membranes from Bacillus subtilis.
Topics: Ascorbic Acid; Bacillus subtilis; Carbon Monoxide; Cell Membrane; Cyanides; Dithionite; Electron Transport Complex IV; Heme; Kinetics; Octoxynol; Oxidation-Reduction; Oxygen; Photolysis; Polyethylene Glycols; Solubility; Spectrophotometry; Tetramethylphenylenediamine | 1993 |
Study of the coordination chemistry of prostaglandin G/H synthase by resonance Raman spectroscopy.
Topics: Animals; Carbon Monoxide; Circular Dichroism; Dithionite; Ferrous Compounds; Heme; Hydrogen Bonding; Male; Molecular Structure; Oxidation-Reduction; Prostaglandin-Endoperoxide Synthases; Protoporphyrins; Seminal Vesicles; Sheep; Spectrophotometry; Spectrum Analysis, Raman | 1996 |
Electron transfer across the O2- generating flavocytochrome b of neutrophils. Evidence for a transition from a low-spin state to a high-spin state of the heme iron component.
Topics: Animals; Arachidonic Acid; Binding Sites; Cattle; Cytochrome b Group; Dithionite; Electron Spin Resonance Spectroscopy; Electron Transport; Flavoproteins; Heme; Hydrogen-Ion Concentration; In Vitro Techniques; NADPH Oxidases; Neutrophils; Nitriles; Oxidation-Reduction; Oxygen; Sodium Dodecyl Sulfate; Spectrophotometry; Superoxides | 1996 |
Probing the heme iron coordination structure of pressure-induced cytochrome P420cam.
Topics: Camphor 5-Monooxygenase; Circular Dichroism; Dithionite; Electron Spin Resonance Spectroscopy; Heme; Iron; Pressure; Protein Conformation; Spectrophotometry, Atomic | 1996 |
Differential characterization of neutrophil cytochrome p30 and cytochrome b-558 by low-temperature absorption and resonance Raman spectroscopies.
Topics: Animals; Cytochrome b Group; Dithionite; Dithiothreitol; Heme; Hydrogen-Ion Concentration; NADPH Oxidases; Neutrophils; Oxidation-Reduction; Peritoneum; Rabbits; Spectrophotometry, Atomic; Spectrum Analysis, Raman | 1997 |
Spontaneous spectral changes of the reduced cytochrome bd.
Topics: Azotobacter vinelandii; Bacillus subtilis; Binding Sites; Carbon Monoxide; Cytochrome b Group; Cytochromes; Dithionite; Electron Transport Chain Complex Proteins; Escherichia coli; Escherichia coli Proteins; Heme; Iron; Kinetics; Models, Chemical; Oxidation-Reduction; Oxidoreductases; Spectrophotometry | 1997 |
The heme component of the neutrophil NADPH oxidase complex is a target for aryliodonium compounds.
Topics: Animals; Biphenyl Compounds; Cattle; Cell Membrane; Cytochrome b Group; Dithionite; Electron Spin Resonance Spectroscopy; Enzyme Inhibitors; Flavin-Adenine Dinucleotide; Heme; NADPH Oxidases; Neutrophils; Onium Compounds; Oxidation-Reduction; Oxygen Consumption; Spectrometry, Fluorescence; Spectrophotometry | 1999 |
Stoichiometric arginine binding in the oxygenase domain of inducible nitric oxide synthase requires a single molecule of tetrahydrobiopterin per dimer.
Topics: Animals; Arginine; Binding Sites; Biopterins; Carbon Monoxide; Chromatography, Gel; Conserved Sequence; Dimerization; Dithionite; Ferrous Compounds; Heme; Mice; Nitric Oxide Synthase; Nitric Oxide Synthase Type II; Oxygenases; Protein Binding; Recombinant Proteins; Spectrophotometry, Ultraviolet; Titrimetry | 1999 |
Biochemical and electrochemical characterization of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans.
Topics: Dithionite; Electrochemistry; Electron Spin Resonance Spectroscopy; Heme; Kinetics; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Periplasm; Quinones; Spectrophotometry, Ultraviolet; Substrate Specificity; Titrimetry | 1999 |
Extended heme promiscuity in the cyanobacterial cytochrome c oxidase: characterization of native complexes containing hemes A, O, and D, respectively.
Topics: Acids; Blotting, Western; Carbon Monoxide; Cell Membrane; Chromatography, High Pressure Liquid; Cyanobacteria; Dithionite; Electron Transport Complex IV; Heme; Hydrogen Peroxide; Intracellular Membranes; NAD; Oxygen; Quaternary Ammonium Compounds; Spectrum Analysis; Thiosulfates | 1999 |
Purification and characterization of a catalase from the facultatively psychrophilic bacterium Vibrio rumoiensis S-1(T) exhibiting high catalase activity.
Topics: Amino Acids; Animals; Catalase; Catalysis; Cattle; Cytoplasm; Dithionite; Enzyme Stability; Heme; Hydrogen Peroxide; Hydrogen-Ion Concentration; Isoelectric Point; Kinetics; Molecular Weight; Periplasm; Spectrum Analysis; Temperature; Vibrio | 2000 |
Heme structure of hemoglobin M Iwate [alpha 87(F8)His-->Tyr]: a UV and visible resonance Raman study.
Topics: Amino Acid Substitution; Dithionite; Heme; Hemoglobin A; Hemoglobin M; Hemoglobins; Histidine; Humans; Methemoglobin; Oxidation-Reduction; Peptide Fragments; Reducing Agents; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Tyrosine | 2000 |
Nitrosyl adducts of FixL as probes of heme environment.
Topics: Bacterial Proteins; Binding Sites; Dithionite; Electron Spin Resonance Spectroscopy; Heme; Hemeproteins; Histidine Kinase; Kinetics; Models, Molecular; Nitric Oxide; Nitroso Compounds; Oxidation-Reduction; Oxygen; Protein Conformation; Protein Structure, Tertiary; Sinorhizobium meliloti; Spectrophotometry; Spectrum Analysis, Raman; Temperature; Thermodynamics | 2000 |
Spectral studies of tert-butyl isothiocyanate-inactivated P450 2E1.
Topics: Animals; Binding Sites; Carbon Monoxide; Chromatography, Liquid; Cytochrome P-450 CYP2E1; Cytochrome P-450 CYP2E1 Inhibitors; Dithionite; Electron Spin Resonance Spectroscopy; Enzyme Activation; Enzyme Inhibitors; Fomepizole; Heme; Iodobenzenes; Isothiocyanates; NADP; Pyrazoles; Rabbits; Rats; Spectrometry, Mass, Electrospray Ionization | 2001 |
Soret-excited Raman spectroscopy of the spinach cytochrome b6f complex. Structures of the b- and c-type hemes, chlorophyll a, and beta-carotene.
Topics: Ascorbic Acid; beta Carotene; Chlorophyll; Chlorophyll A; Cytochrome b Group; Cytochrome b6f Complex; Cytochromes; Cytochromes f; Dithionite; Ferric Compounds; Ferrous Compounds; Heme; Multienzyme Complexes; Oxidation-Reduction; Spectrum Analysis, Raman; Spinacia oleracea | 2001 |
Mapping of heme-binding domains in soluble guanylyl cyclase beta1 subunit.
Topics: Animals; Binding Sites; Brain; Dithionite; Guanylate Cyclase; Heme; Imidazoles; Nitric Oxide; Protein Binding; Protein Interaction Mapping; Protein Structure, Tertiary; Protein Subunits; Rats; Receptors, Cytoplasmic and Nuclear; Recombinant Fusion Proteins; Sequence Deletion; Soluble Guanylyl Cyclase; Spectrum Analysis; Thioredoxins | 2001 |
A physiochemical mechanism of hemozoin (beta-hematin) synthesis by malaria parasite.
Topics: alpha-Linolenic Acid; Aminophenols; Animals; Antioxidants; Dithionite; Dithiothreitol; Free Radicals; Glutathione; Heme; Hemeproteins; Hemin; Linoleic Acid; Lipid Metabolism; Malaria; Mercaptoethanol; Mice; Models, Chemical; Oxygen; Plasmodium yoelii; Reducing Agents; Superoxide Dismutase; Temperature | 2002 |
The reactivity of alpha-hydroxyhaem and verdohaem bound to haem oxygenase-1 to dioxygen and sodium dithionite.
Topics: Carbon Monoxide; Dithionite; Electron Spin Resonance Spectroscopy; Heme; Heme Oxygenase (Decyclizing); Heme Oxygenase-1; Macromolecular Substances; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Oxygen; Porphyrins; Spectrophotometry; Spectrophotometry, Infrared | 2002 |
The naphthoquinol oxidizing cytochrome bc1 complex of the hyperthermophilic knallgasbacterium Aquifex aeolicus: properties and phylogenetic relationships.
Topics: Ascorbic Acid; Bacteria; Bacterial Proteins; Cell Membrane; Dithionite; Electrochemistry; Electron Spin Resonance Spectroscopy; Electron Transport Complex III; Escherichia coli; Heme; Hydroquinones; Iron-Sulfur Proteins; Oxidation-Reduction; Phylogeny; Recombinant Proteins; Spectrophotometry; Titrimetry | 2003 |
A cytochrome b562 variant with a c-type cytochrome CXXCH heme-binding motif as a probe of the Escherichia coli cytochrome c maturation system.
Topics: Amino Acid Motifs; Cysteine; Cytochrome b Group; Cytochromes c; Disulfides; Dithionite; Dithiothreitol; Escherichia coli; Escherichia coli Proteins; Heme; Hemin; Mutation; Plasmids; Protein Binding; Protein Disulfide-Isomerases; Spectrometry, Mass, Electrospray Ionization; Spectrophotometry; Subcellular Fractions | 2003 |
Ability of tetrahydrobiopterin analogues to support catalysis by inducible nitric oxide synthase: formation of a pterin radical is required for enzyme activity.
Topics: Amino Acids; Arginine; Binding Sites; Biopterins; Catalysis; Dithionite; Electron Spin Resonance Spectroscopy; Enzyme Activation; Free Radicals; Freezing; Heme; Nitrates; Nitric Oxide Synthase; Nitric Oxide Synthase Type II; Nitrites; Oxyhemoglobins; Protein Structure, Tertiary; Pterins; Recombinant Proteins; Time Factors | 2003 |
Evidence for two different electron transfer pathways in the same enzyme, nitrate reductase A from Escherichia coli.
Topics: Benzoquinones; Cytochromes; Dithionite; Electron Transport; Escherichia coli; Escherichia coli Proteins; Heme; Nitrate Reductase; Nitrate Reductases; Oxidation-Reduction; Spectrum Analysis; Vitamin K 3 | 2004 |
The redox behavior of the heme in cystathionine beta-synthase is sensitive to pH.
Topics: Circular Dichroism; Citric Acid; Coenzymes; Cystathionine beta-Synthase; Dithionite; Electron Spin Resonance Spectroscopy; Enzyme Activation; Ferric Compounds; Heme; Hemeproteins; Humans; Hydrogen-Ion Concentration; Oxidation-Reduction; Reducing Agents; Spectrophotometry; Spectrum Analysis, Raman | 2004 |
Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site.
Topics: Binding Sites; Catalysis; Cytochrome b Group; Cytochromes; Dithionite; Electron Transport; Electron Transport Chain Complex Proteins; Escherichia coli Proteins; Heme; Membrane Potentials; Oxidation-Reduction; Oxidoreductases | 2005 |
Effects of Y132H and F145L substitutions on the activity, azole resistance and spectral properties of Candida albicans sterol 14-demethylase P450 (CYP51): a live example showing the selection of altered P450 through interaction with environmental compound
Topics: Amino Acid Sequence; Amino Acid Substitution; Antifungal Agents; Azoles; Candida albicans; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Dithionite; Drug Resistance, Microbial; Escherichia coli; Fluconazole; Fungal Proteins; Heme; Oxidoreductases; Spectrum Analysis; Sterol 14-Demethylase | 2005 |
The heme of cystathionine beta-synthase likely undergoes a thermally induced redox-mediated ligand switch.
Topics: Circular Dichroism; Cystathionine beta-Synthase; Dithionite; Enzyme Stability; Ferric Compounds; Ferrous Compounds; Heme; Hot Temperature; Humans; Hydrogen-Ion Concentration; Models, Molecular; Oxidation-Reduction; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Proteins; Spectrum Analysis; Spectrum Analysis, Raman; Temperature | 2005 |
Cardiolipin is associated with the terminal oxidase of an extremely halophilic archaeon.
Topics: Aminoacridines; Cardiolipins; Cell Membrane; Cytochrome b Group; Detergents; Dithionite; Electron Transport Complex IV; Electrophoresis; Halobacteriales; Heme; Oxidation-Reduction; Oxidoreductases; Oxidoreductases, N-Demethylating; Solubility; Spectrometry, Fluorescence | 2007 |
Tricarballylate catabolism in Salmonella enterica. The TcuB protein uses 4Fe-4S clusters and heme to transfer electrons from FADH2 in the tricarballylate dehydrogenase (TcuA) enzyme to electron acceptors in the cell membrane.
Topics: Aconitic Acid; Amino Acid Substitution; Bacterial Proteins; Catalysis; Dithionite; Electrochemistry; Electron Spin Resonance Spectroscopy; Heme; Hydrogen-Ion Concentration; Iron-Sulfur Proteins; Kinetics; Membrane Proteins; Models, Biological; Molecular Weight; Oxidation-Reduction; Oxidoreductases; Recombinant Proteins; Salmonella enterica; Spectrophotometry; Spectrophotometry, Ultraviolet; Sulfur; Temperature; Tricarboxylic Acids | 2007 |
Nitrite reductase activity of hemoglobin S (sickle) provides insight into contributions of heme redox potential versus ligand affinity.
Topics: Allosteric Site; Dithionite; Heme; Hemoglobin A; Hemoglobin, Sickle; Hemoglobins; Humans; Hydrogen-Ion Concentration; Ligands; Models, Biological; Nitric Oxide; Nitrite Reductases; Oxidation-Reduction; Protein Conformation; Protein Structure, Tertiary | 2008 |
ATP-driven reduction by dark-operative protochlorophyllide oxidoreductase from Chlorobium tepidum mechanistically resembles nitrogenase catalysis.
Topics: Adenosine Triphosphate; Catalysis; Chlorobium; Cysteine; Dithionite; Electrons; Escherichia coli; Heme; Kinetics; Leucine; Light; Lysine; Nitrogenase; Oxidoreductases; Protochlorophyllide | 2008 |
Spectral characterization of the recombinant mouse tumor suppressor 101F6 protein.
Topics: Amino Acid Sequence; Animals; Cytochrome b Group; Dithionite; Electron Spin Resonance Spectroscopy; Heme; Membrane Proteins; Mice; Micelles; Oxidation-Reduction; Recombinant Proteins; Saccharomyces; Sequence Homology, Amino Acid; Spectrum Analysis; Spectrum Analysis, Raman; Temperature; Tumor Suppressor Proteins; Ultraviolet Rays | 2010 |
Crystal structure of the carbon monoxide complex of human cytoglobin.
Topics: Animals; Carbon Monoxide; Crystallization; Cytoglobin; Dithionite; Drosophila Proteins; Globins; Heme; Hemoglobins; Humans; Mice; Models, Molecular; Nerve Tissue Proteins; Neuroglobin; Protein Binding; Protein Conformation; X-Ray Diffraction | 2011 |
Radical formation in cytochrome c oxidase.
Topics: Animals; Ascorbic Acid; Binding Sites; Biocatalysis; Cattle; Copper; Dithionite; Electron Spin Resonance Spectroscopy; Electron Transport; Electron Transport Complex IV; Free Radicals; Heme; Hydrogen Peroxide; Hydrogen-Ion Concentration; Models, Chemical; Models, Molecular; Oxidation-Reduction; Oxygen; Peroxides; Protein Binding; Protons; Tyrosine | 2011 |
Reduction of the lipocalin type heme containing protein nitrophorin -- sensitivity of the fold-stabilizing cysteine disulfides toward routine heme-iron reduction.
Topics: Cystine; Dithionite; Glutathione Disulfide; Heme; Hemeproteins; Insect Proteins; Iron; Lipocalins; Molecular Weight; Oxidation-Reduction; Protein Stability; Reducing Agents; Salivary Proteins and Peptides; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Thiosulfates; Titrimetry | 2011 |
Relative importance of driving force and electrostatic interactions in the reduction of multihaem cytochromes by small molecules.
Topics: Cytochrome c Group; Dithionite; Electron Transport; Heme; Hydrogen-Ion Concentration; Osmolar Concentration; Static Electricity; Thermodynamics | 2013 |
A map of dielectric heterogeneity in a membrane protein: the hetero-oligomeric cytochrome b6f complex.
Topics: Circular Dichroism; Cytochrome b6f Complex; Dithionite; Electron Transport; Heme; Membrane Proteins; Oxidation-Reduction; Plant Leaves; Protein Structure, Tertiary; Quinones; Spinacia oleracea; Static Electricity; Temperature | 2014 |
NO2(-)-mediated nitrosylation of ferrous microperoxidase-11.
Topics: Animals; Dithionite; Heme; Horses; Hydrogen-Ion Concentration; Iron; Kinetics; Nitric Oxide; Nitrites; Peroxidases | 2015 |
Calcium ions inhibit reduction of heme a in bovine cytochrome c oxidase.
Topics: Animals; Calcium; Cattle; Dithionite; Dose-Response Relationship, Drug; Electron Transport; Electron Transport Complex IV; Heme; Kinetics; Ruthenium Compounds | 2015 |
The Radical SAM enzyme NirJ catalyzes the removal of two propionate side chains during heme d
Topics: Amino Acid Motifs; Amino Acid Sequence; Bacterial Proteins; Catalysis; Chromatography, High Pressure Liquid; Dithionite; Heme; Iron-Sulfur Proteins; Models, Chemical; Molecular Structure; Mutagenesis, Site-Directed; Nitrate Reductase; Propionates; Recombinant Fusion Proteins; Reducing Agents; Rhodobacteraceae; S-Adenosylmethionine; Sequence Alignment; Sequence Homology, Amino Acid; Species Specificity; Substrate Specificity; Tetrapyrroles | 2017 |