Page last updated: 2024-08-22

molybdenum and heme

molybdenum has been researched along with heme in 52 studies

Research

Studies (52)

TimeframeStudies, this research(%)All Research%
pre-199021 (40.38)18.7374
1990's4 (7.69)18.2507
2000's13 (25.00)29.6817
2010's11 (21.15)24.3611
2020's3 (5.77)2.80

Authors

AuthorsStudies
Johnson, JL; Rajagopalan, KV3
Nason, A; Pan, SS1
Bacchi, CJ; Baker, H; Hutner, SH; Katz, L; Shapiro, A; Tamburro, KO1
Bailey, JL; Borchers, R; Hall, RL; Lorimer, GH; Solomonson, LP1
Brill, AS1
Garner, CD; Hewitt, EJ; Notton, BA1
Asher, SA; Schuster, TM1
Rajagopalan, KV; Southerland, WM; Winge, DR1
Arata, H; Shimizu, M; Takamiya, K1
Fu, YH; Marzluf, GA; Okamoto, PM1
Fukumori, Y; Fukuoka, M; Yamanaka, T1
Barber, MJ; Kay, CJ; Solomonson, LP1
Barber, MJ; Solomonson, LP; Spence, JT1
Bellissimo, D; Crawford, NM; Davis, RW; Smith, M1
McCreery, MJ; Solomonson, LP1
Melcer, I; Orten, JM; Sardesai, VM1
Brown, SB; Jones, P; Prudhoe, K; Suggett, A1
Bray, RC; George, GN; Godfrey, C; Greenwood, C; Thomson, AJ1
Onoue, Y1
Southerland, WM; Toghrol, F1
De la Rosa, MA; Vega, JM; Zumft, WG1
Cannons, AC; Hipkin, CR; Kau, DA1
Hanlon, SP; Holt, RA; McEwan, AG; Solomon, PS; Toh, TH1
Friedrich, CG; Klockenkämper, R; Kostka, S; Kraft, R; Quentmeier, A1
Banerjee, R; Green, EL; Loehr, TM; Taoka, S1
Asso, M; Blasco, F; Giordano, G; Guigliarelli, B; Magalon, A; Rothery, RA1
Blasco, F; Magalon, A; Rothery, RA; Weiner, JH1
Berks, BC; Butler, CS; Cheesman, MR; Ferguson, SJ; Richardson, DJ; Thomson, AJ1
Enemark, JH; Feng, C; Hazzard, JT; Hurley, JK; Rajagopalan, KV; Tollin, G; Wilson, HL1
Cheesman, MR; Hanson, GR; McDevitt, CA; McEwan, AG; Noble, CJ1
Hartson, SD; Huang, W; Leach, N; Matts, RL; Yun, BG1
Bardischewsky, F; Friedrich, CG; Hellwig, P; Kostka, S; Quentmeier, A; Rother, D1
Garner, DK; Lu, Y; Russell, BS; Yeung, N; Zhao, X1
Butler, CS; Dridge, EJ; Jepson, BJ; Line, K; Richardson, DJ; Santini, JM; Watts, CA1
Bernhardt, PV; Creevey, NL; McEwan, AG1
Besson, S; Brondino, CD; Correia, C; Fauque, G; González, PJ; Lampreia, J; Moura, I; Moura, JJ1
Enemark, JH; Johnson-Winters, K; Tollin, G1
Chi, JC; Fischer, K; Krizowski, S; Lambeck, I; Mehlmer, N; Mueller, S; Schwarz, G; Teige, M1
Kappler, U1
Davis, AC; Enemark, JH; Johnson-Winters, K; Nordstrom, AR; Tollin, G1
Berry, RE; Enemark, JH; Meyers, KT; Rajapakshe, A; Tollin, G1
Astashkin, AV; Cornelison, MJ; Enemark, JH; Johnson-Winters, K; Rajapakshe, A1
Curth, U; Herzog, S; Krausze, J; Kruse, T; Mendel, RR; Pierik, AJ; Ringel, P; van den Heuvel, J1
Bernhardt, PV; Fischer-Schrader, K; Kalimuthu, P; Schwarz, G1
Enemark, JH; Kappler, U1
Basu, P; Fischer-Schrader, K; Frizzell, S; Gladwin, MT; Hille, R; Kelley, EE; Krizowski, S; Niks, D; Ragireddy, V; Schwarz, G; Sparacino-Watkins, C; Tejero, J; Wang, J; Wang, L; Zhang, Y1
Wang, Y; Zhang, H; Zhang, T1
Bender, D; Burlina, AB; Kaczmarek, AT; Kuester, S; Schwarz, G1
Bender, D; Eh, M; Kaczmarek, AT; Schwarz, G1
Enemark, JH1

Reviews

6 review(s) available for molybdenum and heme

ArticleYear
Transition metals in biochemistry.
    Molecular biology, biochemistry, and biophysics, 1977, Volume: 26

    Topics: Animals; Binding Sites; Copper; Heme; Humans; Iron; Iron-Sulfur Proteins; Mathematics; Metalloproteins; Metals; Molecular Conformation; Molybdenum; Oxidation-Reduction; Protein Binding; Protein Conformation

1977
The coordination and function of the redox centres of the membrane-bound nitrate reductases.
    Cellular and molecular life sciences : CMLS, 2001, Volume: 58, Issue:2

    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
The diheme cytochrome b subunit (Narl) of Escherichia coli nitrate reductase A (NarGHI): structure, function, and interaction with quinols.
    Journal of molecular microbiology and biotechnology, 2001, Volume: 3, Issue:2

    Topics: Amino Acid Sequence; Cytochrome b Group; Escherichia coli; Guanine Nucleotides; Heme; Hydroquinones; Models, Molecular; Molecular Sequence Data; Molybdenum; Nitrate Reductase; Nitrate Reductases; Organometallic Compounds; Protein Structure, Secondary; Protein Subunits; Sequence Alignment; Sequence Homology, Amino Acid

2001
Elucidating the catalytic mechanism of sulfite oxidizing enzymes using structural, spectroscopic, and kinetic analyses.
    Biochemistry, 2010, Aug-31, Volume: 49, Issue:34

    Topics: Animals; Binding Sites; Catalysis; Coenzymes; Electron Spin Resonance Spectroscopy; Electron Transport; Heme; Humans; Kinetics; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Spectrum Analysis; Sulfite Dehydrogenase; Sulfite Oxidase; Sulfites

2010
Bacterial sulfite-oxidizing enzymes.
    Biochimica et biophysica acta, 2011, Volume: 1807, Issue:1

    Topics: Amino Acid Sequence; Bacteria; Catalytic Domain; Electron Spin Resonance Spectroscopy; Genome, Bacterial; Heme; Humans; Models, Molecular; Molybdenum; Protein Conformation; Protein Folding; Sulfite Dehydrogenase; Sulfite Oxidase; Sulfites

2011
Sulfite-oxidizing enzymes.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2015, Volume: 20, Issue:2

    Topics: Catalysis; Electron Spin Resonance Spectroscopy; Heme; Kinetics; Models, Molecular; Molybdenum; Sulfite Oxidase; Sulfites

2015

Other Studies

46 other study(ies) available for molybdenum and heme

ArticleYear
Tryptic cleavage of rat liver sulfite oxidase. Isolation and characterization of molybdenum and heme domains.
    The Journal of biological chemistry, 1977, Mar-25, Volume: 252, Issue:6

    Topics: Animals; Binding Sites; Crystallization; Electron Spin Resonance Spectroscopy; Heme; Hydrogen-Ion Concentration; Kinetics; Liver; Molecular Weight; Molybdenum; Oxidoreductases; Peptide Fragments; Protein Binding; Protein Conformation; Rats; Spectrophotometry; Spectrophotometry, Ultraviolet; Sulfites; Trypsin

1977
Purification and characterization of homogeneous assimilatory reduced nicotinamide adenine dinucleotide phosphate-nitrate reductase from Neurospora crassa.
    Biochimica et biophysica acta, 1978, Apr-12, Volume: 523, Issue:2

    Topics: Copper; Heme; Iron; Kinetics; Molybdenum; NADP; Neurospora; Neurospora crassa; Nitrate Reductases; Peptide Fragments; Zinc

1978
Dense Crithidia growth and heme sparing: relation to Fe, Cu, Mo chelation.
    The Journal of protozoology, 1978, Volume: 25, Issue:4

    Topics: Animals; Biopterins; Chelating Agents; Copper; Crithidia; Heme; Hydrogen-Ion Concentration; Iron; Molybdenum

1978
Reduced nicotinamide adenine dinucleotide-nitrate reductase of Chlorella vulgaris. Purification, prosthetic groups, and molecular properties.
    The Journal of biological chemistry, 1975, Jun-10, Volume: 250, Issue:11

    Topics: Binding Sites; Centrifugation, Zonal; Chlorella; Chromatography, DEAE-Cellulose; Chromatography, Gel; Cyanides; Flavins; Heme; Iron; Molecular Weight; Molybdenum; NAD; Nitrate Reductases; Oxidation-Reduction; Protein Binding; Protein Conformation; Spectrophotometry; Spectrophotometry, Ultraviolet; Sulfides

1975
Nitrate reductases: properties and possible mechanism.
    Biochemical Society transactions, 1979, Volume: 7, Issue:4

    Topics: Electron Transport; Flavins; Heme; Iron; Kinetics; Molybdenum; Nitrate Reductases; Protein Binding

1979
Resonance Raman examination of axial ligand bonding and spin-state equilibria in metmyoglobin hydroxide and other heme derivatives.
    Biochemistry, 1979, Nov-27, Volume: 18, Issue:24

    Topics: Animals; Heme; Hemeproteins; Iron; Ligands; Mathematics; Metmyoglobin; Molybdenum; Protein Binding; Protein Conformation; Spectrophotometry; Spectrum Analysis, Raman; Whales

1979
The domains of rat liver sulfite oxidase. Proteolytic separation and characterization.
    The Journal of biological chemistry, 1978, Dec-25, Volume: 253, Issue:24

    Topics: Amino Acids; Animals; Chymotrypsin; Circular Dichroism; Heme; Kinetics; Liver; Molecular Weight; Molybdenum; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Papain; Peptide Fragments; Protein Conformation; Rats; Trypsin

1978
Purification and properties of sulfite oxidase from human liver.
    The Journal of clinical investigation, 1976, Volume: 58, Issue:3

    Topics: Animals; Antibodies; Chromatography, Gel; Cross Reactions; Cytochromes; Electrophoresis, Polyacrylamide Gel; Female; Heme; Humans; Liver; Male; Molecular Weight; Molybdenum; Oxidoreductases; Rats

1976
Human sulfite oxidase deficiency. Characterization of the molecular defect in a multicomponent system.
    The Journal of clinical investigation, 1976, Volume: 58, Issue:3

    Topics: Antibody Formation; Antigen-Antibody Complex; Autopsy; Cross Reactions; Deficiency Diseases; Female; Heme; Humans; Liver; Molybdenum; Oxidoreductases; Pregnancy; Xanthine Oxidase

1976
Purification and properties of trimethylamine N-oxide reductase from aerobic photosynthetic bacterium Roseobacter denitrificans.
    Journal of biochemistry, 1992, Volume: 112, Issue:4

    Topics: Bacteria; Bacteria, Aerobic; Bacterial Proteins; Cytochrome c Group; Electrophoresis, Polyacrylamide Gel; Heme; Molecular Weight; Molybdenum; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Photosynthesis; Sensitivity and Specificity; Sodium Dodecyl Sulfate; Spectrophotometry

1992
Nit-3, the structural gene of nitrate reductase in Neurospora crassa: nucleotide sequence and regulation of mRNA synthesis and turnover.
    Molecular & general genetics : MGG, 1991, Volume: 227, Issue:2

    Topics: Amino Acid Sequence; Base Sequence; Blotting, Northern; Flavin-Adenine Dinucleotide; Gene Expression Regulation, Fungal; Genes, Fungal; Heme; Kinetics; Molecular Sequence Data; Molybdenum; Neurospora crassa; Nitrate Reductase; Nitrate Reductases; Nitrates; Restriction Mapping; RNA, Fungal; RNA, Messenger; Sequence Homology, Nucleic Acid

1991
Nitrobacter winogradskyi cytochrome a1c1 is an iron-sulfur molybdoenzyme having hemes a and c.
    Journal of biochemistry, 1987, Volume: 102, Issue:3

    Topics: Cytochromes a1; Cytochromes c1; Electron Spin Resonance Spectroscopy; Heme; Molybdenum; Nitrate Reductases; Nitrobacter; Oxidoreductases; Sulfur; Tungsten

1987
Circular dichroism and potentiometry of FAD, heme and Mo-pterin prosthetic groups of assimilatory nitrate reductase.
    Biochemistry, 1988, Aug-09, Volume: 27, Issue:16

    Topics: Circular Dichroism; Electron Spin Resonance Spectroscopy; Flavin-Adenine Dinucleotide; Heme; Molybdenum; Nitrate Reductase; Nitrate Reductases; Oxidation-Reduction; Potentiometry; Pterins; Spectrum Analysis

1988
Stoichiometry of electron uptake and oxidation-reduction midpoint potentials of NADH:nitrate reductase.
    The Biochemical journal, 1988, Mar-15, Volume: 250, Issue:3

    Topics: Chlorella; Electron Transport; Flavin-Adenine Dinucleotide; Heme; Membrane Potentials; Molybdenum; Nitrate Reductase (NADH); Nitrate Reductases; Oxidation-Reduction

1988
Sequence and nitrate regulation of the Arabidopsis thaliana mRNA encoding nitrate reductase, a metalloflavoprotein with three functional domains.
    Proceedings of the National Academy of Sciences of the United States of America, 1988, Volume: 85, Issue:14

    Topics: Amino Acid Sequence; Base Sequence; Binding Sites; Cytochrome b Group; Cytochrome Reductases; Cytochrome-B(5) Reductase; Cytochromes b5; DNA; Flavin-Adenine Dinucleotide; Heme; Molecular Sequence Data; Molybdenum; Nitrate Reductase; Nitrate Reductases; Nitrates; Nucleic Acid Hybridization; Oxidoreductases Acting on Sulfur Group Donors; Plants; Pterins; RNA, Messenger

1988
Radiation inactivation of assimilatory NADH:nitrate reductase from Chlorella. Catalytic and physical sizes of functional units.
    The Journal of biological chemistry, 1986, Jan-15, Volume: 261, Issue:2

    Topics: Chlorella; Chromatography, Gel; Flavin-Adenine Dinucleotide; Heme; Immunosorbent Techniques; Macromolecular Substances; Mathematics; Molybdenum; Nitrate Reductase; Nitrate Reductases; Structure-Activity Relationship

1986
The effects of certain inorganic ions on in vitro porphyrin--heme formation.
    Biochemical medicine, 1973, Volume: 7, Issue:3

    Topics: Animals; Arsenic; Cattle; Chickens; Cobalt; Copper; Depression, Chemical; Dose-Response Relationship, Drug; Edetic Acid; Erythrocytes; Heme; In Vitro Techniques; Iron; Levulinic Acids; Liver; Molybdenum; Porphyrins; Stimulation, Chemical; Uranium; Zinc

1973
Catalysis by haemin of some molybdenum (VI) oxidations.
    Nature, 1968, Aug-10, Volume: 219, Issue:5154

    Topics: Catalysis; Heme; Hydrogen-Ion Concentration; Kinetics; Molybdenum; Oxidation-Reduction; Spectrophotometry

1968
Electron-paramagnetic-resonance spectroscopy studies on the dissimilatory nitrate reductase from Pseudomonas aeruginosa.
    The Biochemical journal, 1984, Dec-01, Volume: 224, Issue:2

    Topics: Electron Spin Resonance Spectroscopy; Heme; Iron; Molybdenum; Nitrate Reductases; Nitric Oxide; Oxidation-Reduction; Pseudomonas aeruginosa; Sulfur

1984
Sulfite oxidase from Merluccius productus.
    Biochimica et biophysica acta, 1980, Sep-09, Volume: 615, Issue:1

    Topics: Animals; Chemical Phenomena; Chemistry, Physical; Electron Spin Resonance Spectroscopy; Enzyme Inhibitors; Fishes; Heme; Kinetics; Liver; Mitochondria, Liver; Molecular Weight; Molybdenum; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors

1980
Purification of Thiobacillus novellus sulfite oxidase. Evidence for the presence of heme and molybdenum.
    The Journal of biological chemistry, 1983, Jun-10, Volume: 258, Issue:11

    Topics: Heme; Kinetics; Molecular Weight; Molybdenum; Oxidation-Reduction; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Spectrometry, Fluorescence; Spectrophotometry; Thiobacillus

1983
Composition and structure of assimilatory nitrate reductase from Ankistrodesmus braunii.
    The Journal of biological chemistry, 1981, Jun-10, Volume: 256, Issue:11

    Topics: Amino Acids; Chlorophyta; Flavins; Heme; Iron; Kinetics; Macromolecular Substances; Molecular Weight; Molybdenum; Nitrate Reductases; Oxidation-Reduction; Spectrophotometry

1981
Further characterization of the assimilatory nitrate reductase from the yeast Candida nitratophila.
    Journal of general microbiology, 1993, Volume: 139, Issue:3

    Topics: Amino Acid Sequence; Amino Acids; Candida; Heme; Molecular Sequence Data; Molybdenum; Nitrate Reductase; Nitrate Reductases; Osmolar Concentration; Phosphates; Proteins; Trypsin

1993
Dimethylsulfide:acceptor oxidoreductase from Rhodobacter sulfidophilus. The purified enzyme contains b-type haem and a pterin molybdenum cofactor.
    European journal of biochemistry, 1996, Jul-15, Volume: 239, Issue:2

    Topics: Chromatography; Chromatography, Gel; Chromatography, Ion Exchange; Coenzymes; Dimethyl Sulfoxide; Durapatite; Electrophoresis, Polyacrylamide Gel; Heme; Kinetics; Macromolecular Substances; Metalloproteins; Molecular Weight; Molybdenum; Molybdenum Cofactors; Oxidation-Reduction; Oxidoreductases; Pteridines; Rhodobacter; Spectrophotometry; Substrate Specificity

1996
Characterization of a new type of sulfite dehydrogenase from Paracoccus pantotrophus GB17.
    Archives of microbiology, 2000, Volume: 173, Issue:2

    Topics: Amino Acid Sequence; Blotting, Western; Cytochrome c Group; Cytochrome Reductases; Electrophoresis, Polyacrylamide Gel; Heme; Iron; Molecular Sequence Data; Molybdenum; Oxidation-Reduction; Paracoccus; Periplasm; Sulfite Dehydrogenase; Thiosulfates

2000
Resonance Raman characterization of the heme cofactor in cystathionine beta-synthase. Identification of the Fe-S(Cys) vibration in the six-coordinate low-spin heme.
    Biochemistry, 2001, Jan-16, Volume: 40, Issue:2

    Topics: Binding, Competitive; Carbon Monoxide; Cystathionine beta-Synthase; Cysteine; Ferric Compounds; Ferrous Compounds; Heme; Homocysteine; Humans; Iron-Sulfur Proteins; Ligands; Mercuric Chloride; Molybdenum; Oxidation-Reduction; Protein Binding; Pyridoxal Phosphate; Spectrum Analysis, Raman

2001
Assignment of haem ligands and detection of electronic absorption bands of molybdenum in the di-haem periplasmic nitrate reductase of Paracoccus pantotrophus.
    FEBS letters, 2001, Jun-29, Volume: 500, Issue:1-2

    Topics: Amino Acid Sequence; Circular Dichroism; Electron Spin Resonance Spectroscopy; Heme; Molecular Sequence Data; Molybdenum; Nitrate Reductase; Nitrate Reductases; Paracoccus; Sequence Homology, Amino Acid

2001
Role of conserved tyrosine 343 in intramolecular electron transfer in human sulfite oxidase.
    The Journal of biological chemistry, 2003, Jan-31, Volume: 278, Issue:5

    Topics: Amino Acid Substitution; Animals; Binding Sites; Chickens; Conserved Sequence; Electron Transport; Heme; Humans; Hydrogen-Ion Concentration; Hydroxides; Kinetics; Molybdenum; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases Acting on Sulfur Group Donors; Photolysis; Recombinant Proteins; Spectrophotometry; Tyrosine

2003
Characterization of the redox centers in dimethyl sulfide dehydrogenase from Rhodovulum sulfidophilum.
    Biochemistry, 2002, Dec-24, Volume: 41, Issue:51

    Topics: Alcohol Oxidoreductases; Alphaproteobacteria; Bacterial Proteins; Circular Dichroism; Cytochrome b Group; Electron Spin Resonance Spectroscopy; Ferric Compounds; Heme; Iron-Sulfur Proteins; Ligands; Molybdenum; Oxidation-Reduction; Oxidoreductases; Potentiometry; Thermodynamics

2002
Novobiocin induces a distinct conformation of Hsp90 and alters Hsp90-cochaperone-client interactions.
    Biochemistry, 2004, Jun-29, Volume: 43, Issue:25

    Topics: Animals; Autoradiography; Benzoquinones; eIF-2 Kinase; Enzyme Inhibitors; Heme; HSC70 Heat-Shock Proteins; HSP70 Heat-Shock Proteins; HSP90 Heat-Shock Proteins; Humans; Lactams, Macrocyclic; Molecular Chaperones; Molybdenum; Novobiocin; Peptide Mapping; Protein Binding; Protein Conformation; Protein Folding; Quinones; Rabbits; Reticulocytes; Tacrolimus Binding Proteins

2004
Sulfur dehydrogenase of Paracoccus pantotrophus: the heme-2 domain of the molybdoprotein cytochrome c complex is dispensable for catalytic activity.
    Biochemistry, 2005, May-10, Volume: 44, Issue:18

    Topics: Amino Acid Sequence; Bacterial Proteins; Catalysis; Cloning, Molecular; Coenzymes; Cytochrome c Group; Electrochemistry; Flavoproteins; Heme; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Multienzyme Complexes; Oxidoreductases; Paracoccus pantotrophus; Protein Structure, Tertiary; Pteridines; Spectrophotometry, Ultraviolet

2005
Catalytic reduction of NO to N2O by a designed heme copper center in myoglobin: implications for the role of metal ions.
    Journal of the American Chemical Society, 2006, May-31, Volume: 128, Issue:21

    Topics: Catalysis; Copper; Electron Spin Resonance Spectroscopy; Heme; Metals; Molybdenum; Myoglobin; Nitric Oxide; Oxidation-Reduction; Oxidoreductases; Protein Engineering

2006
Investigation of the redox centres of periplasmic selenate reductase from Thauera selenatis by EPR spectroscopy.
    The Biochemical journal, 2007, Nov-15, Volume: 408, Issue:1

    Topics: Cytoplasm; Electron Spin Resonance Spectroscopy; Heme; Iron; Molybdenum; Oxidation-Reduction; Oxidoreductases; Protein Binding; Sulfates; Temperature; Thauera

2007
A mechanistic and electrochemical study of the interaction between dimethyl sulfide dehydrogenase and its electron transfer partner cytochrome c2.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2008, Volume: 13, Issue:8

    Topics: Catalysis; Catalytic Domain; Cytochromes c2; Dimethyl Sulfoxide; Electrochemistry; Electron Transport; Heme; Hydrogen-Ion Concentration; Iron-Sulfur Proteins; Molybdenum; Oxidation-Reduction; Oxidoreductases; Rhodovulum; Sulfides

2008
Biochemical and spectroscopic characterization of the membrane-bound nitrate reductase from Marinobacter hydrocarbonoclasticus 617.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2008, Volume: 13, Issue:8

    Topics: Alteromonadaceae; Cell Membrane; Electron Spin Resonance Spectroscopy; Electrophoresis; Guanine Nucleotides; Heme; Hydrogen-Ion Concentration; Iron; Molecular Weight; Molybdenum; Nitrate Reductase; Oxidation-Reduction; Potentiometry; Pterins; Spectrophotometry, Ultraviolet; Temperature

2008
Kinetic analysis of 14-3-3-inhibited Arabidopsis thaliana nitrate reductase.
    Biochemistry, 2010, Sep-21, Volume: 49, Issue:37

    Topics: 14-3-3 Proteins; Arabidopsis; Catalysis; Coenzymes; Eukaryota; Heme; Kinetics; Metalloproteins; Molybdenum; Molybdenum Cofactors; NAD; Nitrate Reductase; Nitrate Reductase (NADH); Nitrate Reductases; Oxidation-Reduction; Phosphorylation; Protein Kinases; Pteridines

2010
Effects of large-scale amino acid substitution in the polypeptide tether connecting the heme and molybdenum domains on catalysis in human sulfite oxidase.
    Metallomics : integrated biometal science, 2010, Volume: 2, Issue:11

    Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Biocatalysis; Chickens; Coenzymes; Heme; Humans; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Peptides; Pteridines; Sulfite Oxidase

2010
Intramolecular electron transfer in sulfite-oxidizing enzymes: probing the role of aromatic amino acids.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2012, Volume: 17, Issue:3

    Topics: Amino Acids, Aromatic; Catalysis; Catalytic Domain; Electrochemistry; Electrons; Heme; Humans; Models, Biological; Models, Molecular; Molybdenum; Mutation; Recombinant Proteins; Sulfite Oxidase

2012
Determination of the distance between the Mo(V) and Fe(III) heme centers of wild type human sulfite oxidase by pulsed EPR spectroscopy.
    The journal of physical chemistry. B, 2012, Feb-16, Volume: 116, Issue:6

    Topics: Animals; Catalytic Domain; Chickens; Crystallography, X-Ray; Electron Spin Resonance Spectroscopy; Electron Transport; Ferric Compounds; Heme; Humans; Molybdenum; Oxidoreductases Acting on Sulfur Group Donors; Recombinant Proteins; Temperature

2012
Biochemical characterization of molybdenum cofactor-free nitrate reductase from Neurospora crassa.
    The Journal of biological chemistry, 2013, May-17, Volume: 288, Issue:20

    Topics: Amino Acid Sequence; Cloning, Molecular; Coenzymes; Dimerization; Electron Spin Resonance Spectroscopy; Heme; Metalloproteins; Models, Molecular; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; NADP; Neurospora crassa; Nitrate Reductase; Nitrite Reductases; Oxidation-Reduction; Protein Binding; Pteridines; Recombinant Proteins; Sequence Homology, Amino Acid; Ultracentrifugation

2013
Mediated electrochemistry of nitrate reductase from Arabidopsis thaliana.
    The journal of physical chemistry. B, 2013, Jun-27, Volume: 117, Issue:25

    Topics: Anthraquinones; Arabidopsis; Benzyl Viologen; Biocatalysis; Electrochemical Techniques; Electrodes; Electron Transport; Enzymes, Immobilized; Heme; Kinetics; Molybdenum; Nitrate Reductase; Nitrates; Oxidation-Reduction; Paraquat

2013
Sulfite Oxidase Catalyzes Single-Electron Transfer at Molybdenum Domain to Reduce Nitrite to Nitric Oxide.
    Antioxidants & redox signaling, 2015, Aug-01, Volume: 23, Issue:4

    Topics: Coenzymes; Electron Transport; Fibroblasts; Heme; Humans; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitric Oxide; Nitrites; Oxidation-Reduction; Protein Structure, Tertiary; Pteridines; Signal Transduction; Sulfite Oxidase

2015
Mechanistic understanding and binding analysis of two-dimensional MoS
    Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy, 2019, Mar-15, Volume: 211

    Topics: Benzothiazoles; Bilirubin; Circular Dichroism; Disulfides; Glycosylation; Heme; Humans; Models, Molecular; Molybdenum; Nanostructures; Protein Conformation; Serum Albumin, Human; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet

2019
Oxygen and nitrite reduction by heme-deficient sulphite oxidase in a patient with mild sulphite oxidase deficiency.
    Journal of inherited metabolic disease, 2020, Volume: 43, Issue:4

    Topics: Amino Acid Metabolism, Inborn Errors; Catalytic Domain; Coenzymes; Electron Transport; Heme; Humans; Infant; Mitochondria; Molybdenum; Nitrites; Oxidation-Reduction; Oxidoreductases Acting on Sulfur Group Donors; Oxygen; Sulfite Oxidase

2020
Molecular mechanism of intramolecular electron transfer in dimeric sulfite oxidase.
    The Journal of biological chemistry, 2022, Volume: 298, Issue:3

    Topics: Electrons; Heme; Molybdenum; Protein Domains; Sulfite Oxidase; Sulfites

2022
Mechanistic complexities of sulfite oxidase: An enzyme with multiple domains, subunits, and cofactors.
    Journal of inorganic biochemistry, 2023, Volume: 247

    Topics: Animals; Chickens; Ferric Compounds; Heme; Humans; Infant, Newborn; Molybdenum; Oxidoreductases Acting on Sulfur Group Donors; Sulfite Oxidase

2023
chemdatabank.com