heme has been researched along with hexacyanoferrate iii in 16 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (12.50) | 18.7374 |
| 1990's | 8 (50.00) | 18.2507 |
| 2000's | 4 (25.00) | 29.6817 |
| 2010's | 2 (12.50) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Güner, S; Hobbs, DD; Knaff, DB; Kriauciunas, A; Ondrias, MR | 1 |
| Babcock, GT; Hoogland, H; Kean, RT; López-Garriga, JJ; Oertling, WA; Wever, R | 1 |
| Muakkassah, SF; Yang, WC | 1 |
| Adachi, O; Matsushita, K; Takaki, Y; Toyama, H; Yakushi, T | 1 |
| Chapman, SK; Reid, GA; Sharp, RE | 1 |
| Burstyn, JN; Dierks, EA | 1 |
| Lê, KH; Lederer, F; Miles, CS | 1 |
| Pountney, DJ; Raja, KB; Simpson, RJ; Wrigglesworth, JM | 1 |
| Gupte, SA; Phillibert, D; Rupawalla, T; Wolin, MS | 1 |
| Masters, BS; McLain, J; Roman, LJ | 1 |
| MORTON, RK; STURTEVANT, JM | 1 |
| Acker, H; Berchner-Pfannschmidt, U; Bunn, HF; Cross, AR; Fandrey, J; Jackson, TA; Ladoux, A; Larade, K; Lukat-Rodgers, GS; Rodgers, KR; Xie, J; Zhu, H | 1 |
| Higashimoto, Y; Noguchi, M; Palmer, G; Sakamoto, H; Sato, H; Takahashi, K | 1 |
| Cammack, R; Gareta, EG; Marritt, SJ; McKie, AT; Oakhill, JS | 1 |
| Desmet, F; Dewilde, S; Maurelli, S; Moens, L; Tilleman, L; Trandafir, F; Van Doorslaer, S; Verrept, B | 1 |
| Chen, F; Gou, R; Guo, Y; Li, H; Ma, P; Pu, J; Tang, L; Wang, B; Wang, R; Wang, Y; Zheng, B | 1 |
16 other study(ies) available for heme and hexacyanoferrate iii
| Article | Year |
|---|---|
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 |
Metal-ligand vibrations of cyanoferric myeloperoxidase and cyanoferric horseradish peroxidase: evidence for a constrained heme pocket in myeloperoxidase.
Topics: Binding Sites; Ferricyanides; Heme; Horseradish Peroxidase; Humans; Hydrogen Bonding; Molecular Structure; Peroxidase; Spectrum Analysis, Raman | 1990 |
Mechanism of the inhibitory action of phenelzine on microsomal drug metabolism.
Topics: Aminopyrine N-Demethylase; Animals; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Ferricyanides; Heme; Male; Microsomes, Liver; Phenelzine; Phenylhydrazines; Rats; Rats, Inbred Strains; Spectrophotometry | 1981 |
Generation mechanism and purification of an inactive form convertible in vivo to the active form of quinoprotein alcohol dehydrogenase in Gluconobacter suboxydans.
Topics: Acetobacteraceae; Aerobiosis; Alcohol Oxidoreductases; Carbonyl Cyanide m-Chlorophenyl Hydrazone; Cell Membrane; Coenzymes; Culture Media; Enzyme Activation; Ferricyanides; Glycerol; Heme; Hydrogen-Ion Concentration; Kanamycin; Methylphenazonium Methosulfate; Molecular Weight; Oxidation-Reduction; PQQ Cofactor; Protein Conformation; Quinolones; Sorbitol; Ubiquinone; Uncoupling Agents | 1995 |
Modulation of flavocytochrome b2 intraprotein electron transfer via an interdomain hinge region.
Topics: Amino Acid Sequence; Base Sequence; Catalysis; DNA Primers; Electron Transport; Escherichia coli; Ferricyanides; Flavin Mononucleotide; Heme; Kinetics; L-Lactate Dehydrogenase; L-Lactate Dehydrogenase (Cytochrome); Lactates; Lactic Acid; Models, Chemical; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Saccharomyces cerevisiae | 1996 |
The deactivation of soluble guanylyl cyclase by redox-active agents.
Topics: Animals; Cattle; Cyclic GMP; Enzyme Activation; Ferricyanides; Guanylate Cyclase; Heme; Kinetics; Methylene Blue; Nitrates; Nitric Oxide; Oxidation-Reduction; Solubility | 1998 |
Probing intramolecular electron transfer within flavocytochrome b2 with a monoclonal antibody.
Topics: Animals; Antibodies, Monoclonal; Binding Sites; Cytochrome c Group; Electron Transport; Epitopes; Escherichia coli; Ferricyanides; Heme; Immunochemistry; Kinetics; L-Lactate Dehydrogenase; L-Lactate Dehydrogenase (Cytochrome); Mice; Models, Molecular; Pichia; Protein Conformation; Recombinant Proteins; Saccharomyces cerevisiae | 1998 |
The ferric-reducing activity of duodenal brush-border membrane vesicles is associated with a b-type haem.
Topics: Animals; Duodenum; Ferricyanides; Heme; Microvilli; NAD; Oxidation-Reduction; Rabbits | 1999 |
NADPH and heme redox modulate pulmonary artery relaxation and guanylate cyclase activation by NO.
Topics: Animals; Cattle; Colforsin; Cyclic GMP; Electron Transport; Enzyme Activation; Enzyme Inhibitors; Ferricyanides; Flavoproteins; Glutathione; Guanylate Cyclase; Heme; In Vitro Techniques; NADH, NADPH Oxidoreductases; NADP; Nitric Oxide; Oxadiazoles; Oxidation-Reduction; Penicillamine; Pentose Phosphate Pathway; Pulmonary Artery; Quinoxalines; Reactive Oxygen Species; Sulfhydryl Compounds | 1999 |
Chimeric enzymes of cytochrome P450 oxidoreductase and neuronal nitric-oxide synthase reductase domain reveal structural and functional differences.
Topics: Calmodulin; Codon; Cytochrome c Group; DNA; Electron Transport; Ferricyanides; Flavins; Heme; NADPH-Ferrihemoprotein Reductase; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Phosphorylation; Plasmids; Protein Binding; Protein Structure, Tertiary; Recombinant Fusion Proteins; Spectrophotometry; Structure-Activity Relationship | 2003 |
KINETIC INVESTIGATIONS OF YEAST L-LACTATE DEHYDROGENASE (CYTOCHROME B2). I. THE DEHYDROGENATION OF L-LACTATE IN THE PRESENCE AND ABSENCE OF FERRICYANIDE AS ELECTRON ACCEPTOR.
Topics: Catalysis; Cytochromes; Electrons; Ferricyanides; Ferrocyanides; Flavin Mononucleotide; Heme; L-Lactate Dehydrogenase; L-Lactate Dehydrogenase (Cytochrome); Lactates; Lactic Acid; Oxidation-Reduction; Research; Saccharomyces | 1964 |
NCB5OR is a novel soluble NAD(P)H reductase localized in the endoplasmic reticulum.
Topics: Animals; Base Sequence; Blotting, Western; Calreticulin; Cell Line; Chromatography, High Pressure Liquid; Computational Biology; COS Cells; Cytochrome-B(5) Reductase; Cytochromes b5; Cytochromes c; Dose-Response Relationship, Drug; Endoplasmic Reticulum; Female; Ferricyanides; Heme; Humans; Kinetics; Liver; Methemoglobin; Mice; Microscopy, Confocal; Molecular Sequence Data; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Oxygen; Phenotype; Photons; Protein Structure, Tertiary; Recombinant Proteins; Sequence Homology, Nucleic Acid; Spectrum Analysis, Raman; Subcellular Fractions; Superoxides; Time Factors; Transfection; Ultraviolet Rays | 2004 |
The reactions of heme- and verdoheme-heme oxygenase-1 complexes with FMN-depleted NADPH-cytochrome P450 reductase. Electrons required for verdoheme oxidation can be transferred through a pathway not involving FMN.
Topics: Animals; Binding Sites; Deferoxamine; Ferricyanides; Flavin Mononucleotide; Heme; Heme Oxygenase-1; Humans; Models, Chemical; Models, Molecular; Mutation; NADPH-Ferrihemoprotein Reductase; Rats | 2006 |
Functional characterization of human duodenal cytochrome b (Cybrd1): Redox properties in relation to iron and ascorbate metabolism.
Topics: Aminolevulinic Acid; Animals; Ascorbic Acid; Baculoviridae; Cell Line; Cloning, Molecular; Cytochrome b Group; Duodenum; Electron Spin Resonance Spectroscopy; Ferricyanides; Genetic Vectors; Heme; Histidine; Humans; Iron; Ligands; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases; Potentiometry; Recombinant Proteins; Transduction, Genetic | 2008 |
Marked difference in the electronic structure of cyanide-ligated ferric protoglobins and myoglobin due to heme ruffling.
Topics: Animals; Electron Spin Resonance Spectroscopy; Electrons; Escherichia coli; Ferricyanides; Globins; Heme; Horses; Ligands; Methanosarcina; Myoglobin; Phenylalanine; Protein Conformation; Recombinant Proteins; Thermodynamics | 2012 |
The FNR modules contribute to control nitric oxide synthase catalysis revealed by chimera enzymes.
Topics: Animals; Biocatalysis; Cytochromes c; Ferredoxin-NADP Reductase; Ferricyanides; Flavins; Heme; Kinetics; NADP; Nitric Oxide; Nitric Oxide Synthase; Oxidation-Reduction; Oxygenases; Rats; Recombinant Fusion Proteins; Spectrum Analysis; Time Factors | 2017 |