heme has been researched along with sulfur in 89 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 31 (34.83) | 18.7374 |
| 1990's | 4 (4.49) | 18.2507 |
| 2000's | 21 (23.60) | 29.6817 |
| 2010's | 23 (25.84) | 24.3611 |
| 2020's | 10 (11.24) | 2.80 |
| Authors | Studies |
|---|---|
| Aparicio, PJ; Knaff, DB; Malkin, R | 1 |
| Cammack, R; Hewitt, EJ; Hucklesby, DP | 1 |
| de Matteis, F; Gibbs, AH; Järvisalo, J | 1 |
| Hagen, WR; Pierik, AJ | 1 |
| Kato, Y; Kimura, R; Konishi, S; Yamada, S | 1 |
| Fukumori, Y; Fukuoka, M; Yamanaka, T | 1 |
| Gavrikova, EV; Ledenev, AN; Tushurashvili, PR; Vinogradov, AD | 1 |
| Berzofsky, JA; Blumberg, WE; Peisach, J | 1 |
| Clegg, RA; Garland, PB | 1 |
| Kamen, MD; Kennel, SJ; Meyer, TE; Tedro, SM | 1 |
| Ke, B | 1 |
| Dutton, PL; Leigh, JS | 1 |
| Beinert, H; Hansen, RE; Orme-Johnson, NR | 1 |
| Clark, C; Holtzman, JL; Montgomery, MR | 1 |
| Bryant, MP; Varel, VH | 1 |
| Berzofsky, JA; Horecker, BL; Peisach, J | 1 |
| Bissell, DM; Hammaker, L; Schmid, R | 1 |
| Gibson, QH; Jenkins, T; Nagel, RL | 1 |
| Lederer, F; Tarin, J | 1 |
| Rogers, LA; Trüper, HG | 1 |
| Nanzyo, N; Sano, S | 1 |
| Chang, Y; Morell, DB | 1 |
| Blair, DF; Brudvig, GW; Chan, SI | 1 |
| Bray, RC; George, GN; Godfrey, C; Greenwood, C; Thomson, AJ | 1 |
| Christner, JA; Janick, PA; Münck, E; Siegel, LM | 1 |
| Cammack, R; Cole, JA; Cornish-Bowden, A; Jackson, RH | 1 |
| Janick, PA; Siegel, LM | 1 |
| Cammack, R; Crowe, BA; Owen, P | 1 |
| Hatchikian, EC; Zeikus, JG | 1 |
| Holm, RH; Paech, C; Reynolds, JG; Singer, TP | 1 |
| Bukovska, G; Kery, V; Kraus, JP | 1 |
| Dailey, HA; Johnson, MK; Sellers, VM | 1 |
| Tai, CH; Yu, CA; Yu, L; Zhang, L | 1 |
| Finkelstein, JD | 1 |
| Ishimori, K; Morishima, I; Takahashi, S; Yoshioka, S | 1 |
| Janosík, M; Kery, V; Kraus, JP; Maclean, KN; Oliveriusová, J | 1 |
| Asso, M; Blasco, F; Giordano, G; Guigliarelli, B; Magalon, A; Rothery, RA | 1 |
| Brinkmann, H; Eilers, T; Hänsch, R; Hille, R; Koch, B; Mendel, RR; Nieder, J; Richter, T; Schwarz, G; Witt, C | 1 |
| Chapman, SK; Miles, CS; Munro, AW; Murdoch, J; Ost, TW; Reid, GA | 1 |
| Babcock, GT; Berka, V; Schelvis, JP; Tsai, AL | 1 |
| Foster, MW; McMahon, TJ; Stamler, JS | 1 |
| Lochner, M; Meuwly, M; Woggon, WD | 1 |
| HANSEN, RE; RIESKE, JS; ZAUGG, WS | 1 |
| DERVARTANIAN, DV; VEEGER, C; ZEYLEMAKER, WP | 1 |
| CHAIX, P; FLAMENS, P | 1 |
| Albrecht, T; Bandeiras, TM; Gomes, CM; Kletzin, A; Leal, SS; Rachel, R; Scholz, C; Teixeira, M; Urich, T; Zimmermann, P | 1 |
| Coelho, R; Frazao, C; Kletzin, A; Urich, T | 1 |
| Borel, F; de Groot, A; de Rosny, E; Fontecilla-Camps, JC; Gaillard, J; Jouve, HM; Jullian-Binard, C; Pebay-Peyroula, E | 1 |
| Dahl, C; Lübbe, YJ; Timkovich, R; Youn, HS | 1 |
| Wilson, RB | 1 |
| Cooper, RM; Cornelis, P; Jackson, RW; Laus, G; Matthijs, S; Tehrani, KA | 1 |
| Escalante-Semerena, JC; Lewis, JA | 1 |
| Dombek, KM; Liu, JC; McKnight, SL; Mohler, RE; Synovec, RE; Tu, BP; Young, ET | 1 |
| Bernhardt, PV; Hanson, GR; Kappler, U; Kilmartin, J; McKenzie, KJ; Riley, MJ; Teschner, J | 1 |
| Archer, M; Matias, PM; Oliveira, TF; Pereira, IA; Venceslau, SS; Vonrhein, C | 1 |
| Dutka, M; Froncisz, W; Osyczka, A; Sarewicz, M | 1 |
| Crooks, DR; Ghosh, MC; Haller, RG; Rouault, TA; Tong, WH | 1 |
| Oelmüller, R; Sherameti, I; Tripathy, BC | 1 |
| Dahl, C; Grein, F; Hildebrandt, P; Pereira, IA; Schneider, L; Todorovic, S; Venceslau, SS | 1 |
| Dawson, JH; Perera, R; Sono, M; Voegtle, HL | 1 |
| Beckerich, JM; Casaregola, S; Hébert, A | 1 |
| Butt, JN; Einsle, O; Hermann, B; Kern, M; Simon, J | 1 |
| Antipov, AN; Tishkov, VI | 1 |
| Goldberg, DP; McQuilken, AC | 1 |
| Berks, BC; Bradley, JM; Butt, JN; Cheesman, MR; Haynes, K; Hemmings, AM; Kihlken, MA; Marritt, SJ | 1 |
| Kamimura, K; Kanao, T; Kikumoto, M; Nogami, S; Takada, J | 1 |
| Lup, D; Lupan, A; Makarov, SV; Silaghi-Dumitrescu, R; Surducan, M | 1 |
| Dlouhy, AC; Outten, CE | 1 |
| Filipovic, MR; Ivanović-Burmazović, I; Kenkel, I; Miljkovic, JLj | 1 |
| Bhave, G; Borza, DB; Chetyrkin, SV; Clark, TA; Fidler, AL; Hudson, BG; Hudson, JK; Ivy, MT; McDonald, WH; Pedchenko, VK; Rose, KL; Steele, RE; Stothers, CL; Vanacore, RM; Yin, VP | 1 |
| Ajili, Y; Ben Yaghlane, S; Francisco, JS; Hochlaf, M; Jaidane, NE; Mogren Al-Mogren, M; Trabelsi, T | 1 |
| Cabello-Donayre, M; Campos-Salinas, J; Gálvez, FJ; Koeller, DM; Malagarie-Cazenave, S; Martínez-García, M; Orrego, LM; Pérez-Victoria, JM; Pineda-Molina, E; Sánchez-Cañete, MP | 1 |
| Arman, HD; Chee-Garza, M; Meininger, DJ; Tonzetich, ZJ | 1 |
| Andjus, P; Bačić, G; Jovanović, M; Mojović, M; Popović-Bijelić, A; Selaković, V; Stamenković, S | 1 |
| Manz, DH; Paul, BT; Torti, FM; Torti, SV | 1 |
| Iqbal, N; Kaur, P; Sharma, P; Sharma, S; Singh, AK; Singh, PK; Singh, TP; Sirohi, HV | 1 |
| Farmer, PJ; Kumar, MR | 1 |
| Bes, MT; Fillat, MF; González, A; Peleato, ML; Sevilla, E | 1 |
| Jadhav, S; Philpott, CC | 1 |
| Crosson, S; Fiebig, A; Stein, BJ | 1 |
| Ghiaccio, V; La, P; Oved, JH; Rivella, S | 1 |
| Bollinger, JM; Krebs, C; Liu, G; Maio, N; Rouault, TA; Sil, D; Tong, WH | 1 |
| Dailey, HA; Medlock, AE; Weerth, RS | 1 |
| Jiang, M; Li, B; Li, J; Liang, M; Pang, Y; Tan, G; Wang, J; Wang, X; Wu, X; Yue, G; Zhu, L | 1 |
| Balwani, M; Fanelli, MJ; Gouya, L; Longo, N; Petrides, PE; Phillips, J; Plutzky, J; Rhyee, S; Sardh, E; Sweetser, MT; Ventura, P | 1 |
| Bird, LJ; Eddie, BJ; Glaven, SM; Malanoski, AP; Martínez-Pérez, C; Mussmann, M; Pelikan, C; Pinamang, P | 1 |
| Abdullah, Y; Adlung, L; Altamura, S; Andrieux, G; Boehm, ME; Boerries, M; Busch, H; Chakraborty, S; Gröne, HJ; Helm, B; Kastl, P; Klingmüller, U; Lehmann, WD; Muckenthaler, MU; Schilling, M; Schwarzmüller, LE; Wagner, MC | 1 |
| Arora, A; Dutta, D; Kalita, A; Kumar, V; Mishra, RK | 1 |
| Ali, MY; Flor, S; Griguer, CE; Oliva, CR | 1 |
11 review(s) available for heme and sulfur
| Article | Year |
|---|---|
The primary electron acceptor of photosystem. I.
Topics: Aniline Compounds; Chloroplasts; Cytochromes; Darkness; Electron Spin Resonance Spectroscopy; Electron Transport; Ferredoxins; Heme; Kinetics; Light; Models, Biological; Oxidation-Reduction; Oxygen; Phenazines; Photochemistry; Photosynthesis; Plant Cells; Plants; Potentiometry; Quantum Theory; Spectrophotometry; Spectrophotometry, Ultraviolet; Sulfur; Temperature; Time Factors | 1973 |
Pathways and regulation of homocysteine metabolism in mammals.
Topics: Animals; Cystathionine; Cystathionine beta-Synthase; Cystathionine gamma-Lyase; Cysteine; Heme; Homocysteine; Isoenzymes; Kinetics; Mammals; Methionine; Methionine Adenosyltransferase; Organ Specificity; Oxidation-Reduction; Pyridoxal Phosphate; S-Adenosylhomocysteine; S-Adenosylmethionine; Sulfur; Tetrahydrofolates | 2000 |
The coordination and function of the redox centres of the membrane-bound nitrate reductases.
Topics: Cell Membrane; Coenzymes; Electron Spin Resonance Spectroscopy; Electron Transport; Escherichia coli; Heme; Iron; Molybdenum; Mutagenesis, Site-Directed; Nitrate Reductase; Nitrate Reductases; Oxidation-Reduction; Protein Subunits; Sulfur | 2001 |
S-nitrosylation in health and disease.
Topics: Copper; Cysteine; Disease; Heme; Humans; Nitric Oxide; Nitric Oxide Synthase; Nitrites; Nitroso Compounds; Oxidation-Reduction; Sulfur | 2003 |
Iron dysregulation in Friedreich ataxia.
Topics: Amino Acid Sequence; Animals; Frataxin; Friedreich Ataxia; Heme; Humans; Iron; Iron Metabolism Disorders; Iron-Binding Proteins; Manganese; Mice; Mice, Knockout; Mitochondria; Mitochondrial Diseases; Molecular Sequence Data; Oxygen Consumption; Sulfur; Superoxide Dismutase | 2006 |
Siroheme: an essential component for life on earth.
Topics: Adaptation, Physiological; Heme; Nitrogen; Oxidation-Reduction; Oxidoreductases; Plant Development; Plants; Signal Transduction; Sulfur | 2010 |
Physiological function and catalytic versatility of bacterial multihaem cytochromes c involved in nitrogen and sulfur cycling.
Topics: Bacteria; Biocatalysis; Cytochromes c; Heme; Nitrogen; Nitrogen Cycle; Sulfur | 2011 |
Mitochondria and Iron: current questions.
Topics: Animals; Biological Transport; Carrier Proteins; Disease Susceptibility; Heme; Humans; Iron; Mitochondria; Neoplasms; Protein Binding; Sulfur | 2017 |
Redox-Based Transcriptional Regulation in Prokaryotes: Revisiting Model Mechanisms.
Topics: Bacterial Proteins; Biomarkers; Heme; Iron; Models, Biological; NAD; Oxidants; Oxidation-Reduction; Prokaryotic Cells; Protein Binding; Protein Interaction Domains and Motifs; Reactive Nitrogen Species; Reactive Oxygen Species; Sensitivity and Specificity; Structure-Activity Relationship; Sulfur; Transcription Factors; Transcription, Genetic | 2019 |
The ins and outs of iron: Escorting iron through the mammalian cytosol.
Topics: Animals; Cytosol; Heme; Humans; Iron; Iron-Binding Proteins; Iron-Sulfur Proteins; Metalloproteins; Molecular Chaperones; Sulfur | 2019 |
Mitoferrin, Cellular and Mitochondrial Iron Homeostasis.
Topics: Heme; Homeostasis; Humans; Iron; Mitochondria; Sulfur | 2022 |
78 other study(ies) available for heme and sulfur
| 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 |
Electron-paramagnetic-resonance studies of the mechanism of leaf nitrite reductase. Signals from the iron-sulphur centre and haem under turnover conditions.
Topics: Electron Spin Resonance Spectroscopy; Heme; Iron; NADH, NADPH Oxidoreductases; Nitrite Reductases; Oxidation-Reduction; Plants; Sulfur | 1978 |
Accelerated conversion of heme to bile pigments caused in the liver by carbon disulfide and other sulfur-containing chemicals.
Topics: Animals; Bile Pigments; Carbon Disulfide; Cycloheximide; Cytochrome P-450 Enzyme System; Heme; Liver; Male; Microsomes, Liver; Mixed Function Oxygenases; Phenobarbital; Rats; Sulfur | 1978 |
S = 9/2 EPR signals are evidence against coupling between the siroheme and the Fe/S cluster prosthetic groups in Desulfovibrio vulgaris (Hildenborough) dissimilatory sulfite reductase.
Topics: Desulfovibrio; Electron Spin Resonance Spectroscopy; Heme; Iron; Oxidoreductases Acting on Sulfur Group Donors; Spectroscopy, Mossbauer; Sulfur; Temperature | 1991 |
Effects of sulfur-containing metabolites of hexachlorobenzene on the heme metabolic enzymes in rat liver.
Topics: 5-Aminolevulinate Synthetase; Animals; Chlorobenzenes; Drug Administration Schedule; Female; Heme; Hexachlorobenzene; Liver; Pentachlorophenol; Porphyrins; Rats; Rats, Inbred Strains; Sulfones; Sulfur; Tissue Distribution | 1990 |
Nitrobacter winogradskyi cytochrome a1c1 is an iron-sulfur molybdoenzyme having hemes a and c.
Topics: Cytochromes a1; Cytochromes c1; Electron Spin Resonance Spectroscopy; Heme; Molybdenum; Nitrate Reductases; Nitrobacter; Oxidoreductases; Sulfur; Tungsten | 1987 |
Studies on the succinate dehydrogenating system. Isolation and properties of the mitochondrial succinate-ubiquinone reductase.
Topics: Animals; Binding Sites; Cattle; Electron Spin Resonance Spectroscopy; Electron Transport Complex II; Electrophoresis, Polyacrylamide Gel; Flavins; Heme; Iron; Kinetics; Mitochondria, Heart; Multienzyme Complexes; Octoxynol; Oxidation-Reduction; Oxidoreductases; Polyethylene Glycols; Spectrophotometry; Substrate Specificity; Succinate Dehydrogenase; Succinates; Succinic Acid; Sulfur; Ubiquinone | 1985 |
Sulfheme proteins. I. Optical and magnetic properties of sulfmyoglobin and its derivatives.
Topics: Absorption; Animals; Azides; Cetacea; Chemical Phenomena; Chemistry; Computers; Cyanides; Electron Spin Resonance Spectroscopy; Fluorides; Heme; Hydrogen-Ion Concentration; Infrared Rays; Iron; Myoglobin; Porphyrins; Protein Binding; Pyrroles; Quaternary Ammonium Compounds; Spectrophotometry; Spectrum Analysis; Sulfides; Sulfur | 1971 |
Non-haem iron and the dissociation of piericidin A sensitivity from site 1 energy conservation in mitochondria from Torulopsis utilis.
Topics: Chloramphenicol; Cycloheximide; Cytochromes; Electron Transport; Energy Transfer; Erythromycin; Flavoproteins; Glycerol; Heme; Iron; Iron Isotopes; Malates; Mitochondria; Mitosporic Fungi; NAD; Oxygen Consumption; Proteins; Pyridines; Pyruvates; Rotenone; Sulfur; Tetracycline; Time Factors | 1971 |
Iron protein content of Thiocapsapfennigii, a purple sulfur bacterium of atypical chlorophyll composition.
Topics: Amino Acid Sequence; Amino Acids; Bacteria; Bacterial Proteins; Chlorophyll; Chromatography, DEAE-Cellulose; Chromatography, Gel; Cytochrome c Group; Electrophoresis, Polyacrylamide Gel; Ferredoxins; Heme; Iron; Sodium Dodecyl Sulfate; Solubility; Spectrophotometry; Spectrophotometry, Ultraviolet; Sulfur | 1973 |
Electron spin resonance characterization of Chromatium D hemes, non-heme irons and the components involved in primary photochemistry.
Topics: Anaerobiosis; Bacterial Chromatophores; Chromatium; Cytochromes; Electron Spin Resonance Spectroscopy; Electron Transport; Energy Transfer; Heme; Iron; Kinetics; Metalloproteins; Models, Biological; Oxidation-Reduction; Photophosphorylation; Potentiometry; Sodium Dodecyl Sulfate; Solubility; Spectrophotometry; Sulfur; Temperature; Time Factors | 1973 |
Electron paramagnetic resonance-detectable electron acceptors in beef heart mitochondria. Ubihydroquinone-cytochrome c reductase segment of the electron transfer system and complex mitochondrial fragments.
Topics: Animals; Cattle; Cold Temperature; Cytochrome c Group; Cytochrome Reductases; Cytochromes; Electron Spin Resonance Spectroscopy; Electron Transport; Heme; Iron; Metalloproteins; Mitochondria, Muscle; Myocardium; NAD; Oxidation-Reduction; Subcellular Fractions; Succinate Dehydrogenase; Sulfites; Sulfur; Ubiquinone | 1974 |
Iron species of hepatic microsomes from control and phenobarbital-treated rats.
Topics: Animals; Calcium; Chromatography, Affinity; Cytochrome P-450 Enzyme System; Cytochromes; Ferritins; Heme; Horses; Iron; Male; Metalloproteins; Microsomes, Liver; Phenobarbital; Potassium Chloride; Rats; Sulfur; Time Factors; Ultracentrifugation | 1974 |
Nutritional features of Bacteroides fragilis subsp. fragilis.
Topics: Anaerobiosis; Bacteroides; Bicarbonates; Carbon Dioxide; Culture Media; Cysteine; Glucose; Heme; Methionine; Minerals; Nitrogen; Quaternary Ammonium Compounds; Species Specificity; Sulfides; Sulfur; Vitamin B 12 | 1974 |
Sulfheme proteins. IV. The stoichiometry of sulfur incorporation and the isolation of sulfhemin, the prosthetic group of sulfmyoglobin.
Topics: Butanones; Chromatography, Paper; Drug Stability; Heme; Iron; Kinetics; Mercury; Myoglobin; Oxidation-Reduction; Oxygen; Peroxides; Protein Binding; Pyridines; Solubility; Spectrophotometry; Sulfides; Sulfur; Sulfur Isotopes; Temperature | 1972 |
Liver sinusoidal cells. Identification of a subpopulation for erythrocyte catabolism.
Topics: Animals; Autoradiography; Carbon; Cell Survival; Erythrocytes; Gold Colloid, Radioactive; Heme; Hot Temperature; Liver; Male; Microsomes, Liver; Oxygenases; Peroxidases; Phagocytosis; Pronase; Rats; Rats, Inbred Strains; Serum Albumin, Radio-Iodinated; Spleen; Sulfur; Technetium | 1972 |
Ligand binding in hemoglobin J Capetown.
Topics: Binding Sites; Carbon Monoxide; Glutamine; Haptoglobins; Heme; Hemoglobins, Abnormal; Humans; Hydrogen-Ion Concentration; Kinetics; Leucine; Molecular Biology; Oxygen; Sulfur | 1971 |
Chemical modification of the thioether bridges in cytochrome c. A novel method for heme cleavage.
Topics: Acetates; Animals; Binding Sites; Chemical Phenomena; Chemistry; Cytochromes; Ethers; Heme; Horses; Hydrogen-Ion Concentration; Iodine; Iodine Isotopes; Oxidation-Reduction; Peptides; Sulfur; Urea | 1971 |
Purification and properties of adenylyl sulfate reductase from the phototrophic sulfur bacterium, Thiocapsa roseopersicina.
Topics: Adenosine Monophosphate; Ammonium Sulfate; Bacteria; Cell-Free System; Chemical Precipitation; Chromatography, Ion Exchange; Culture Media; Cytochromes; Electron Transport; Ferricyanides; Flavins; Heme; Hot Temperature; Hydrogen-Ion Concentration; Iron; Light; Molecular Weight; Nucleotides; Oxidoreductases; Species Specificity; Spectrophotometry; Sulfates; Sulfhydryl Reagents; Sulfides; Sulfur; Ultracentrifugation; Ultrasonics; Vibration | 1971 |
Type c ferri- and ferrohemochrome formation between hemin c, amino acids, and peptides.
Topics: Amino Acids; Ammonia; Arginine; Cytochromes; Detergents; Glycine; Heme; Histidine; Hydrogen-Ion Concentration; Imidazoles; Indoles; Iron; Lysine; Methionine; Peptides; Pigments, Biological; Porphyrins; Protein Binding; Spectrophotometry; Sulfur; Tryptophan | 1968 |
The structure of the chromophore of sulphmyoglobin.
Topics: Chemical Phenomena; Chemistry; Heme; Myoglobin; Peroxidases; Pyridines; Spectrophotometry; Sulfur | 1967 |
Electron spin relaxation of CuA and cytochrome a in cytochrome c oxidase. Comparison to heme, copper, and sulfur radical complexes.
Topics: Animals; Cattle; Copper; Cytochrome a Group; Cytochromes; Electron Spin Resonance Spectroscopy; Electron Transport Complex IV; Free Radicals; Heme; Kinetics; Laccase; Mathematics; Myocardium; Oxidoreductases; Sulfur; Temperature | 1984 |
Electron-paramagnetic-resonance spectroscopy studies on the dissimilatory nitrate reductase from Pseudomonas aeruginosa.
Topics: Electron Spin Resonance Spectroscopy; Heme; Iron; Molybdenum; Nitrate Reductases; Nitric Oxide; Oxidation-Reduction; Pseudomonas aeruginosa; Sulfur | 1984 |
Mössbauer spectroscopic studies of Escherichia coli sulfite reductase. Evidence for coupling between the siroheme and Fe4S4 cluster prosthetic groups.
Topics: Electron Spin Resonance Spectroscopy; Escherichia coli; Heme; Iron; Iron-Sulfur Proteins; Metalloproteins; Oxidation-Reduction; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Protein Conformation; Spectrum Analysis; Sulfur | 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 |
Electron paramagnetic resonance and optical evidence for interaction between siroheme and Fe4S4 prosthetic groups in complexes of Escherichia coli sulfite reductase hemoprotein with added ligands.
Topics: Arsenic; Arsenites; Carbon Monoxide; Cyanides; Dimethyl Sulfoxide; Electron Spin Resonance Spectroscopy; Escherichia coli; Ferrous Compounds; Guanidines; Heme; Iron; Ligands; Oxidation-Reduction; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Spectrophotometry; Sulfides; Sulfite Reductase (NADPH); Sulfur; Urea | 1983 |
Study of the respiratory chain in Micrococcus luteus (lysodeikticus) by electron-spin-resonance spectroscopy.
Topics: Bacterial Proteins; Cell Membrane; Copper; Electron Spin Resonance Spectroscopy; Electron Transport; Heme; Iron; Membrane Potentials; Membrane Proteins; Micrococcus; Oxidation-Reduction; Solubility; Sulfur | 1983 |
Characterization of a new type of dissimilatory sulfite reductase present in Thermodesulfobacterium commune.
Topics: Amino Acid Sequence; Amino Acids; Bacteria; Carbon Monoxide; Heme; Iron; Kinetics; Macromolecular Substances; Molecular Weight; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Spectrophotometry; Sulfur | 1983 |
Structural identification of iron-sulfur clusters of the respiratory chain-linked NADH dehydrogenase.
Topics: Anaerobiosis; Animals; Cattle; Cytochrome Reductases; Flavin Mononucleotide; Fourier Analysis; Heme; Iron; Iron-Sulfur Proteins; Macromolecular Substances; Magnetic Resonance Spectroscopy; Metalloproteins; Mitochondria, Heart; NADH Dehydrogenase; Protein Conformation; Spectrophotometry; Sulfur | 1981 |
Transsulfuration depends on heme in addition to pyridoxal 5'-phosphate. Cystathionine beta-synthase is a heme protein.
Topics: Animals; Cystathionine; Cystathionine beta-Synthase; Escherichia coli; Heme; Hemeproteins; Homocysteine; Humans; Kinetics; Liver; Pyridoxal Phosphate; Rats; Recombinant Proteins; Serine; Spectrophotometry; Sulfur | 1994 |
Function of the [2FE-2S] cluster in mammalian ferrochelatase: a possible role as a nitric oxide sensor.
Topics: Animals; Binding Sites; Electron Spin Resonance Spectroscopy; Ferrochelatase; Heme; Humans; In Vitro Techniques; Iron; Mice; Molecular Sequence Data; Molecular Structure; Nitric Oxide; Recombinant Proteins; Saccharomyces cerevisiae; Sequence Homology, Amino Acid; Spectrophotometry; Spectrophotometry, Ultraviolet; Sulfur; Tumor Cells, Cultured | 1996 |
pH-induced intramolecular electron transfer between the iron-sulfur protein and cytochrome c(1) in bovine cytochrome bc(1) complex.
Topics: Animals; Cattle; Cytochromes c1; Electron Transport; Electron Transport Complex III; Heme; Hydrogen-Ion Concentration; Iron; Iron-Sulfur Proteins; Oxidation-Reduction; Polyenes; Stilbenes; Sulfur; Thiazoles; Time Factors | 2000 |
Roles of the axial push effect in cytochrome P450cam studied with the site-directed mutagenesis at the heme proximal site.
Topics: Binding Sites; Camphor; Camphor 5-Monooxygenase; Cysteine; Electrons; Escherichia coli; Ferricyanides; Ferrous Compounds; Heme; Hydroxylation; Magnetic Resonance Spectroscopy; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Oxygen; Plasmids; Protein Conformation; Protons; Spectrophotometry; Sulfur | 2000 |
Transsulfuration in Saccharomyces cerevisiae is not dependent on heme: purification and characterization of recombinant yeast cystathionine beta-synthase.
Topics: Amino Acid Sequence; Catalysis; Cell Division; Cloning, Molecular; Cystathionine beta-Synthase; DNA, Complementary; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Heme; Humans; Kinetics; Ligands; Mass Spectrometry; Molecular Sequence Data; Pyridoxal Phosphate; Recombinant Proteins; S-Adenosylmethionine; Saccharomyces cerevisiae; Sequence Homology, Amino Acid; Sulfur; Time Factors; Ultraviolet Rays | 2000 |
Identification and biochemical characterization of Arabidopsis thaliana sulfite oxidase. A new player in plant sulfur metabolism.
Topics: Amino Acid Sequence; Animals; Arabidopsis; Blotting, Western; Chickens; Coenzymes; Dose-Response Relationship, Drug; Electron Spin Resonance Spectroscopy; Gene Library; Heme; Humans; Kinetics; Metalloproteins; Molecular Sequence Data; Molybdenum Cofactors; Nicotiana; Open Reading Frames; Oxidation-Reduction; Oxidoreductases Acting on Sulfur Group Donors; Peroxisomes; Plasmids; Protein Structure, Tertiary; Pteridines; Recombinant Proteins; Sequence Homology, Amino Acid; Subcellular Fractions; Sulfur; Time Factors; Ultraviolet Rays | 2001 |
Phenylalanine 393 exerts thermodynamic control over the heme of flavocytochrome P450 BM3.
Topics: Amino Acid Sequence; Bacterial Proteins; Carbon Monoxide; Cytochrome P-450 Enzyme System; Escherichia coli; Fatty Acids; Heme; Iron; Kinetics; Mixed Function Oxygenases; Molecular Sequence Data; Mutation; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Oxygen; Phenylalanine; Potentiometry; Sequence Homology, Amino Acid; Sulfur; Thermodynamics; Titrimetry | 2001 |
Resonance Raman detection of the Fe-S bond in endothelial nitric oxide synthase.
Topics: Cell Line; Cysteine; Endothelium; Heme; Iron; Nitric Oxide Synthase; Nitric Oxide Synthase Type III; Spectrum Analysis, Raman; Sulfur | 2002 |
The origin of the low-spin character of the resting state of cytochrome P450cam investigated by means of active site analogues.
Topics: Barium Compounds; Binding Sites; Camphor 5-Monooxygenase; Crown Ethers; Electron Spin Resonance Spectroscopy; Heme; Hydrogen Bonding; Indicators and Reagents; Iron; Models, Chemical; Oxidation-Reduction; Solvents; Sulfur; Water | 2003 |
STUDIES ON THE ELECTRON TRANSFER SYSTEM. LIX. DISTRIBUTION OF IRON AND OF THE COMPONENT GIVING AN ELECTRON PARAMAGNETIC RESONANCE SIGNAL AT G = 1.90 IN SUBFRACTIONS OF COMPLEX 3.
Topics: Animals; Ascorbic Acid; Cattle; Electron Spin Resonance Spectroscopy; Electron Transport; Electron Transport Complex IV; Electrons; Flavins; Heme; Iron; Mitochondria; Myocardium; Proteins; Research; Succinates; Sulfur; Ubiquinone | 1964 |
THE AMOUNT OF NON-HAEM IRON AND ACID-LABILE SULPHUR IN PURIFIED PIG-HEART SUCCINATE DEHYDROGENASE.
Topics: Animals; Chemistry Techniques, Analytical; Electron Spin Resonance Spectroscopy; Electron Transport Complex II; Heart; Heme; Iron; Myocardium; Research; Succinate Dehydrogenase; Sulfur; Swine | 1965 |
[The sulfur-removing ability of some homolactic microorganisms when provided and when not provided with hematin ferments].
Topics: Acetobacter; Bioreactors; Fermentation; Heme; Hemin; Lactobacillus; Sulfur | 1952 |
The sulphur oxygenase reductase from Acidianus ambivalens is a multimeric protein containing a low-potential mononuclear non-haem iron centre.
Topics: Acidianus; Amino Acid Sequence; Archaeal Proteins; Bacterial Proteins; Dimerization; Electron Spin Resonance Spectroscopy; Escherichia coli; Gene Expression Regulation, Enzymologic; Heme; Iron; Microscopy, Electron; Molecular Sequence Data; Multienzyme Complexes; Oxidation-Reduction; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Protein Conformation; Protein Denaturation; Protein Structure, Secondary; Recombinant Fusion Proteins; Substrate Specificity; Sulfur | 2004 |
The sulfur oxygenase reductase from Acidianus ambivalens is an icosatetramer as shown by crystallization and Patterson analysis.
Topics: Acidianus; Antigens, Differentiation, T-Lymphocyte; Archaeal Proteins; Cell Size; Crystallization; Escherichia coli; Heme; Inducible T-Cell Co-Stimulator Protein; Molecular Weight; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Sulfur | 2005 |
Drosophila nuclear receptor E75 is a thiolate hemoprotein.
Topics: Alanine; Amino Acid Sequence; Animals; Cysteine; DNA-Binding Proteins; Drosophila melanogaster; Drosophila Proteins; Electron Spin Resonance Spectroscopy; Gene Expression; Heme; Hemeproteins; Histidine; Humans; Ligands; Molecular Sequence Data; Mutation; Protein Binding; Protein Structure, Tertiary; Receptors, Cytoplasmic and Nuclear; Sequence Alignment; Solubility; Spectrophotometry, Ultraviolet; Sulfur; Transcription Factors | 2006 |
Siro(haem)amide in Allochromatium vinosum and relevance of DsrL and DsrN, a homolog of cobyrinic acid a,c-diamide synthase, for sulphur oxidation.
Topics: Bacterial Proteins; Chromatiaceae; Chromatography; Chromatography, High Pressure Liquid; Gene Deletion; Genetic Complementation Test; Glutamate Synthase; Heme; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Oxidoreductases Acting on Sulfur Group Donors; Recombinant Proteins; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Sulfur | 2006 |
Thioquinolobactin, a Pseudomonas siderophore with antifungal and anti-Pythium activity.
Topics: Antifungal Agents; DNA Transposable Elements; Heme; Hydrolysis; Molecular Sequence Data; Mutation; Oligopeptides; Phenotype; Pseudomonas fluorescens; Pythium; Quinolines; Siderophores; Sulfur | 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 |
Cyclic changes in metabolic state during the life of a yeast cell.
Topics: Acetyl Coenzyme A; Gene Expression Regulation, Fungal; Genes, Fungal; Heme; NADP; Saccharomyces cerevisiae; Sulfur; Time Factors | 2007 |
SoxAX cytochromes, a new type of heme copper protein involved in bacterial energy generation from sulfur compounds.
Topics: Alphaproteobacteria; Bacterial Proteins; Coenzymes; Copper; Cytochrome c Group; Energy Metabolism; Glutathione; Heme; Oxidation-Reduction; Oxidoreductases; Recombinant Proteins; Spectrum Analysis; Sulfur Compounds | 2008 |
The crystal structure of Desulfovibrio vulgaris dissimilatory sulfite reductase bound to DsrC provides novel insights into the mechanism of sulfate respiration.
Topics: Carrier Proteins; Catalytic Domain; Cell Membrane; Crystallography, X-Ray; Cysteine; Desulfovibrio vulgaris; Heme; Iron-Sulfur Proteins; Models, Molecular; Molecular Conformation; Oxidoreductases Acting on Sulfur Group Donors; Protein Binding; Protein Structure, Tertiary; Sulfates; Sulfites; Sulfur | 2008 |
Magnetic interactions sense changes in distance between heme b(L) and the iron-sulfur cluster in cytochrome bc(1).
Topics: Binding Sites; Catalytic Domain; Electron Spin Resonance Spectroscopy; Electron Transport Complex III; Heme; Iron; Models, Molecular; Oxidation-Reduction; Rhodobacter capsulatus; Sulfur | 2009 |
Posttranslational stability of the heme biosynthetic enzyme ferrochelatase is dependent on iron availability and intact iron-sulfur cluster assembly machinery.
Topics: Anemia, Iron-Deficiency; Animals; Biopsy; Cell Line, Tumor; Erythrocytes; Ferrochelatase; Gene Expression Regulation, Enzymologic; Heme; Humans; Iron; Iron Regulatory Protein 2; Leukemia, Erythroblastic, Acute; Mice; Mice, Mutant Strains; Mitochondrial Myopathies; Muscle, Skeletal; Oxidative Stress; Protein Processing, Post-Translational; RNA Processing, Post-Transcriptional; RNA, Messenger; Sulfur | 2010 |
DsrJ, an essential part of the DsrMKJOP transmembrane complex in the purple sulfur bacterium Allochromatium vinosum, is an unusual triheme cytochrome c.
Topics: Bacterial Proteins; Catalysis; Chromatiaceae; Cytochrome c Group; Cytochromes c; Desulfovibrio vulgaris; Electron Spin Resonance Spectroscopy; Electron Transport; Heme; Mutagenesis, Site-Directed; Oxidation-Reduction; Sulfur | 2010 |
Molecular basis for the inability of an oxygen atom donor ligand to replace the natural sulfur donor heme axial ligand in cytochrome P450 catalysis. Spectroscopic characterization of the Cys436Ser CYP2B4 mutant.
Topics: Animals; Aryl Hydrocarbon Hydroxylases; Carbon Monoxide; Circular Dichroism; Cysteine; Cytochrome P450 Family 2; Heme; Iron; Ligands; Models, Molecular; Nitrogen Oxides; Oxygen; Point Mutation; Spectrophotometry; Sulfur | 2011 |
Biodiversity in sulfur metabolism in hemiascomycetous yeasts.
Topics: Amino Acids, Sulfur; Biodiversity; Cysteine; Genetic Variation; Glucosephosphate Dehydrogenase; Glutathione; Heme; Homocysteine; Methionine; NADP; Phylogeny; Sequence Alignment; Sequence Analysis, Protein; Sulfur; Yeasts | 2011 |
Isolation and preliminary characterization of new cytochrome c from autotrophic haloalkaliphilic sulfur-oxidizing bacterium Thioalkalivibrio nitratireducens.
Topics: Amino Acid Sequence; Bacterial Proteins; Circular Dichroism; Cytochromes c; Ectothiorhodospiraceae; Electron Spin Resonance Spectroscopy; Heme; Molecular Sequence Data; Molecular Weight; Oxidation-Reduction; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Sulfur | 2012 |
Sulfur oxygenation in biomimetic non-heme iron-thiolate complexes.
Topics: Biomimetic Materials; Catalytic Domain; Coordination Complexes; Crystallography, X-Ray; Ferric Compounds; Ferrous Compounds; Heme; Hydro-Lyases; Molecular Conformation; Oxidoreductases; Oxygen; Sulfhydryl Compounds; Sulfur | 2012 |
Redox and chemical activities of the hemes in the sulfur oxidation pathway enzyme SoxAX.
Topics: Bacterial Proteins; Catalysis; Catalytic Domain; Cytochrome c Group; Heme; Kinetics; Oxidation-Reduction; Oxidoreductases; Rhodovulum; Sulfur | 2012 |
Tetrathionate-forming thiosulfate dehydrogenase from the acidophilic, chemolithoautotrophic bacterium Acidithiobacillus ferrooxidans.
Topics: Acidithiobacillus; Cloning, Molecular; Enzyme Stability; Escherichia coli; Ferrous Compounds; Gene Expression; Heme; Hydrogen-Ion Concentration; Molecular Weight; Open Reading Frames; Oxidoreductases; Recombinant Proteins; Spectrum Analysis; Sulfur; Temperature; Tetrathionic Acid | 2013 |
Electromerism and linkage isomerism in biologically-relevant Fe-SO complexes.
Topics: Catalytic Domain; Coordination Complexes; Heme; Iron; Isomerism; Models, Chemical; Models, Molecular; Oxides; Oxidoreductases Acting on Sulfur Group Donors; Quantum Theory; Sulfur Compounds; Thermodynamics | 2013 |
The iron metallome in eukaryotic organisms.
Topics: Animals; Heme; Iron; Iron-Sulfur Proteins; Mitochondria; Saccharomyces cerevisiae; Sulfur | 2013 |
Generation of HNO and HSNO from nitrite by heme-iron-catalyzed metabolism with H₂S.
Topics: Electron Spin Resonance Spectroscopy; Heme; Human Umbilical Vein Endothelial Cells; Humans; Hydrogen Sulfide; Iron; Mitochondria; Nitric Oxide; Nitrites; Nitrogen Oxides; Nitrous Acid; Porphyrins; Sulfur Compounds | 2013 |
A unique covalent bond in basement membrane is a primordial innovation for tissue evolution.
Topics: Amino Acid Sequence; Animals; Basement Membrane; Biological Evolution; Collagen Type IV; Cross-Linking Reagents; Drosophila melanogaster; Extracellular Matrix; Extracellular Matrix Proteins; Heme; Imines; Mass Spectrometry; Molecular Sequence Data; Peptides; Peroxidase; Peroxidases; Peroxidasin; Protein Structure, Tertiary; Sequence Analysis, RNA; Sequence Homology, Amino Acid; Sulfur Compounds; Zebrafish | 2014 |
Characterization and reactivity of the weakly bound complexes of the [H, N, S](-) anionic system with astrophysical and biological implications.
Topics: Anions; Astronomical Phenomena; Catalysis; Electrons; Heme; Hydrogen; Nitrites; Nitrogen; Spectrum Analysis; Sulfur | 2015 |
LmABCB3, an atypical mitochondrial ABC transporter essential for Leishmania major virulence, acts in heme and cytosolic iron/sulfur clusters biogenesis.
Topics: Animals; ATP-Binding Cassette Transporters; Heme; Humans; Iron; Leishmania major; Leishmaniasis; Male; Mice; Mice, Inbred C57BL; Mitochondria; Models, Molecular; Protein Transport; Sulfur; Virulence | 2016 |
Gallium(III) Tetraphenylporphyrinates Containing Hydrosulfide and Thiolate Ligands: Structural Models for Sulfur-Bound Iron(III) Hemes.
Topics: Crystallography, X-Ray; Ferric Compounds; Gallium; Heme; Hydrogen Sulfide; Ligands; Models, Molecular; Porphyrins; Sulfhydryl Compounds; Sulfur | 2016 |
Iron-sulfur cluster damage by the superoxide radical in neural tissues of the SOD1(G93A) ALS rat model.
Topics: Amyotrophic Lateral Sclerosis; Animals; Electron Spin Resonance Spectroscopy; Electron Transport Complex IV; Heme; Humans; Iron; Oxidation-Reduction; Oxidative Stress; Rats; Rats, Transgenic; Sulfur; Superoxide Dismutase-1; Superoxides | 2016 |
Design of anti-thyroid drugs: Binding studies and structure determination of the complex of lactoperoxidase with 2-mercaptoimidazole at 2.30 Å resolution.
Topics: Binding Sites; Crystallography, X-Ray; Ethylenethiourea; Heme; Humans; Lactoperoxidase; Methimazole; Protein Conformation; Substrate Specificity; Sulfur; Thyroid Gland; Thyroid Hormones | 2017 |
Chemical trapping and characterization of small oxoacids of sulfur (SOS) generated in aqueous oxidations of H
Topics: Biomimetics; Chromatography, Liquid; Globins; Heme; Hydrogen Sulfide; Keto Acids; Mass Spectrometry; Oxidation-Reduction; Sulfenic Acids; Sulfinic Acids; Sulfur Compounds; Vitamin B 12; Water | 2018 |
Feedback Control of a Two-Component Signaling System by an Fe-S-Binding Receiver Domain.
Topics: Bacterial Proteins; Caulobacter crescentus; Gene Expression Regulation, Bacterial; Heme; Histidine Kinase; Homeostasis; Iron; Kinetics; Phosphorylation; Signal Transduction; Sulfur | 2020 |
Mitochondria Biogenesis Modulates Iron-Sulfur Cluster Synthesis to Increase Cellular Iron Uptake.
Topics: 3T3-L1 Cells; 5-Aminolevulinate Synthetase; Animals; Biological Transport; Erythroid Cells; Erythropoiesis; Gene Expression Regulation; Heme; Hemoglobins; Humans; Iron; Mice; Organelle Biogenesis; Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha; Sulfur | 2020 |
Heme biosynthesis depends on previously unrecognized acquisition of iron-sulfur cofactors in human amino-levulinic acid dehydratase.
Topics: Amino Acid Motifs; Biosynthetic Pathways; Cell Line; Coenzymes; Cysteine; Heme; Humans; Iron; Iron-Sulfur Proteins; Porphobilinogen Synthase; Recombinant Proteins; Sulfur | 2020 |
Ironing out the distribution of [2Fe-2S] motifs in ferrochelatases.
Topics: Actinobacteria; Amino Acid Motifs; Bacterial Proteins; Ferrochelatase; Heme; Iron; Sulfur | 2021 |
ISCA2 deficiency leads to heme synthesis defects and impaired erythroid differentiation in K562 cells by indirect ROS-mediated IRP1 activation.
Topics: 5-Aminolevulinate Synthetase; Aconitate Hydratase; Heme; Humans; Iron; Iron Regulatory Protein 1; Iron-Sulfur Proteins; K562 Cells; Reactive Oxygen Species; Sulfur | 2022 |
Hyperhomocysteinemia in acute hepatic porphyria (AHP) and implications for treatment with givosiran.
Topics: Clinical Trials as Topic; Cystathionine beta-Synthase; Folic Acid; Heme; Homocysteine; Humans; Hyperhomocysteinemia; Methionine; Porphyrias, Hepatic; Pyridoxine; RNA, Small Interfering; Sulfur; Vitamin B 6 | 2022 |
Conservation of Energetic Pathways for Electroautotrophy in the Uncultivated Candidate Order
Topics: Carbon Dioxide; Chromatiaceae; Cytochromes; Heme; Iron; Oxidoreductases; Sulfur | 2022 |
Erythropoietin-driven dynamic proteome adaptations during erythropoiesis prevent iron overload in the developing embryo.
Topics: Erythropoiesis; Erythropoietin; Female; Heme; Hemoglobins; Humans; Iron; Iron Overload; Pregnancy; Proteome; Sulfur | 2022 |
An Intrinsic Alkalization Circuit Turns on
Topics: Ammonia; Escherichia coli; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Glutamate-Ammonia Ligase; Heme; Iron; Ligands; Manganese; Membrane Transport Proteins; Riboswitch; Sulfur | 2022 |