Page last updated: 2024-08-23

sulfur and pteridines

sulfur has been researched along with pteridines in 48 studies

Research

Studies (48)

TimeframeStudies, this research(%)All Research%
pre-19905 (10.42)18.7374
1990's11 (22.92)18.2507
2000's21 (43.75)29.6817
2010's10 (20.83)24.3611
2020's1 (2.08)2.80

Authors

AuthorsStudies
Augier, V; Blasco, F; Chippaux, M; Giordano, G; Pommier, J1
Bauder, R; Lingens, F; Tshisuaka, B1
Johnson, JL; Rajagopalan, KV; Wuebbens, MM1
Gheller, SF; Hedman, B; Hodgson, KO; Lough, SM; McDonald, JW; Newton, WE1
Bublitz, C1
Cotton, RG1
Kaufman, J; Macon, JB; Wolfenden, R1
Johnson, JL; Mize, C; Rajagopalan, KV1
Hagen, WR; Hansen, TA; Hensgens, CM1
Rajagopalan, KV; Wuebbens, MM1
Johnson, JL; Pitterle, DM; Rajagopalan, KV1
Blasco, F; Giordano, G; Magalon, A; Rothery, RA; Weiner, JH1
Hasona, A; Ray, RM; Shanmugam, KT1
Dismukes, GC; Gladyshev, VN; Khangulov, SV; Stadtman, TC1
de Vries, S; Duine, JA; Luykx, DM1
Klipp, W; Leimkühler, S1
Fujiwara, T; Sakurai, T; Yoshimatsu, K1
Amrani, L; Arcangeli, L; Finnerty, V; Glatigny, A; Primus, J; Scazzocchio, C1
Brinkmann, H; Eilers, T; Hänsch, R; Hille, R; Koch, B; Mendel, RR; Nieder, J; Richter, T; Schwarz, G; Witt, C1
Akisu, M; Arslanoglu, S; Ciriş, M; Coker, M; Darcan, S; Demirtaş, E; Gökşen, D; Kultursay, N; Tütüncüoglu, S; Yalaz, M1
Ackerley, C; Becker, L; Salman, MS; Senger, C1
Hänsch, R; Mendel, RR1
Fluhr, R; Sagi, M; Scazzocchio, C1
Dobbek, H; Gremer, L; Huber, R; Kiefersauer, R; Meyer, O1
Holm, RH; Zhang, Y1
Fischer, B; Mendel, RR; Nimtz, M; Otte, T; Santamaria-Araujo, JA; Schwarz, G; Wray, V1
Ahlrichs, R; Coucouvanis, D; Han, J; Nava, P1
Hecht, HJ; Kuper, J; Llamas, A; Mendel, RR; Schwarz, G1
Enemark, JH; Joshi, HK1
Nichols, JD; Rajagopalan, KV1
Bray, RC; Eisenthal, R; Godber, BL; Harrison, R; Lowe, DJ; Mendel, RR; Schwarz, G1
Bhachu, TS; Garner, CD; Hillier, IH; McNamara, JP1
Leimkühler, S; Magalon, A; Neumann, M; Stöcklein, W; Walburger, A1
Daniels, JN; Rajagopalan, KV; Schindelin, H; Wuebbens, MM1
Chowdhury, MM; Hänzelmann, P; Lee, EY; Leimkühler, S; Nimtz, M; Schindelin, H; Schmitz, J1
Leimkühler, S; Marelja, Z; Nimtz, M; Stöcklein, W1
Dean, DR; Dos Santos, PC1
Esaki, N; Kurihara, T; Leimkühler, S; Mihara, H; Urban, A; Zhang, W1
Drew, SC; Friedrich, CG; Lubitz, W; Quentmeier, A; Reijerse, E; Rother, D1
Mihara, H1
Bühning, M; Dahl, JU; Denis, Y; Iobbi-Nivol, C; Jourlin-Castelli, C; Leichert, LI; Leimkühler, S; Méjean, V; Nimtz, M; Radon, C1
Kana, BD; Mizrahi, V; Williams, M1
Baumann, O; Dosche, C; Hille, C; Leimkühler, S; Löhmannsröben, HG; Marelja, Z; Mullick Chowdhury, M1
Kozmin, SG; Schaaper, RM; Stepchenkova, EI1
Black, KA; Dos Santos, PC1
Magalon, A; Mendel, RR1
Beilschmidt, L; Bühning, M; Leimkühler, S1
Maruyama-Nakashita, A; Nakai, Y1

Reviews

7 review(s) available for sulfur and pteridines

ArticleYear
Molybdoenzymes and molybdenum cofactor in plants.
    Journal of experimental botany, 2002, Volume: 53, Issue:375

    Topics: Abscisic Acid; Aldehyde Oxidase; Aldehyde Oxidoreductases; Arabidopsis Proteins; Coenzymes; Enzymes; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Nitrate Reductase; Nitrate Reductases; Oxidoreductases Acting on Sulfur Group Donors; Plants; Pteridines; Sulfur; Xanthine Dehydrogenase

2002
[Discovery and molecular function analysis of sulfur- and selenium-eliminating enzymes crucial for biosynthesis of iron-sulfur clusters and selenoproteins].
    Seikagaku. The Journal of Japanese Biochemical Society, 2011, Volume: 83, Issue:11

    Topics: Animals; Coenzymes; Cystathionine gamma-Lyase; Humans; Iron-Sulfur Proteins; Lyases; Metalloproteins; Molybdenum Cofactors; Pteridines; RNA, Transfer; Selenium; Selenoproteins; Sulfides; Sulfur

2011
Molybdenum cofactor: a key component of Mycobacterium tuberculosis pathogenesis?
    Critical reviews in microbiology, 2014, Volume: 40, Issue:1

    Topics: Biosynthetic Pathways; Carbon; Coenzymes; Enzymes; Metalloproteins; Molybdenum Cofactors; Mycobacterium tuberculosis; Nitrogen; Oxidation-Reduction; Pteridines; Sulfur; Virulence Factors

2014
Shared-intermediates in the biosynthesis of thio-cofactors: Mechanism and functions of cysteine desulfurases and sulfur acceptors.
    Biochimica et biophysica acta, 2015, Volume: 1853, Issue:6

    Topics: Bacterial Proteins; Biosynthetic Pathways; Carbon-Sulfur Lyases; Coenzymes; Cysteine; Iron-Sulfur Proteins; Metalloproteins; Models, Molecular; Molybdenum Cofactors; Protein Structure, Tertiary; Pteridines; Pyridoxal Phosphate; Sulfur

2015
Biosynthesis and Insertion of the Molybdenum Cofactor.
    EcoSal Plus, 2015, Volume: 6, Issue:2

    Topics: Archaea; Bacteria; Biocatalysis; Coenzymes; Enzymes; Escherichia coli; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitrogenase; Pteridines; Pterins; Sulfur; Tungsten

2015
Shared Sulfur Mobilization Routes for tRNA Thiolation and Molybdenum Cofactor Biosynthesis in Prokaryotes and Eukaryotes.
    Biomolecules, 2017, 01-14, Volume: 7, Issue:1

    Topics: Animals; Coenzymes; Escherichia coli; Escherichia coli Proteins; Humans; Metalloproteins; Models, Molecular; Molybdenum Cofactors; Protein Biosynthesis; Pteridines; RNA, Bacterial; RNA, Transfer; Sulfur

2017
Biosynthesis of Sulfur-Containing Small Biomolecules in Plants.
    International journal of molecular sciences, 2020, May-14, Volume: 21, Issue:10

    Topics: Biosynthetic Pathways; Carbon-Sulfur Lyases; Coenzymes; Iron-Sulfur Proteins; Metalloproteins; Molybdenum Cofactors; Plants; Pteridines; Sulfhydryl Compounds; Sulfur; Sulfurtransferases

2020

Other Studies

41 other study(ies) available for sulfur and pteridines

ArticleYear
Involvement of the narJ or narW gene product in the formation of active nitrate reductase in Escherichia coli.
    Molecular microbiology, 1992, Volume: 6, Issue:2

    Topics: Blotting, Western; Coenzymes; Escherichia coli; Gene Expression; Iron; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitrate Reductases; Operon; Plasmids; Pteridines; Spectrometry, Fluorescence; Sulfur; Trypsin

1992
Microbial metabolism of quinoline and related compounds. VII. Quinoline oxidoreductase from Pseudomonas putida: a molybdenum-containing enzyme.
    Biological chemistry Hoppe-Seyler, 1990, Volume: 371, Issue:12

    Topics: Coenzymes; Flavin-Adenine Dinucleotide; Flavoproteins; Iron; Metalloproteins; Molecular Weight; Molybdenum; Molybdenum Cofactors; Oxidoreductases; Oxidoreductases Acting on CH-CH Group Donors; Pseudomonas; Pteridines; Soil Microbiology; Spectrophotometry; Sulfur

1990
The structure of a molybdopterin precursor. Characterization of a stable, oxidized derivative.
    The Journal of biological chemistry, 1989, Aug-15, Volume: 264, Issue:23

    Topics: Alkaline Phosphatase; Animals; Chickens; Coenzymes; Escherichia coli; Intestines; Magnetic Resonance Spectroscopy; Mass Spectrometry; Metalloproteins; Molecular Structure; Molybdenum; Molybdenum Cofactors; Mutation; Phosphorus; Pteridines; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Sulfur

1989
Elicitation of thiomolybdates from the iron-molybdenum cofactor of nitrogenase. Comparison with synthetic Fe-Mo-S complexes.
    European journal of biochemistry, 1986, Aug-15, Volume: 159, Issue:1

    Topics: Azotobacter; Coenzymes; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nitrogenase; Oxidation-Reduction; Oxidoreductases; Pteridines; Spectrophotometry; Sulfur

1986
A direct assay for liver phenylalanine hydroxylase.
    Biochimica et biophysica acta, 1969, Nov-04, Volume: 191, Issue:2

    Topics: Alcohols; Animals; Catalase; Chemical Phenomena; Chemistry; Colorimetry; Fluorometry; Hydrogen-Ion Concentration; Kinetics; Liver; Methods; Mixed Function Oxygenases; Oxygen; Partial Pressure; Phenylalanine; Pteridines; Rats; Sulfur

1969
Phenylalanine hydroxylase of Macaca irus. Purification of two components of the enzyme.
    Biochimica et biophysica acta, 1971, Apr-14, Volume: 235, Issue:1

    Topics: Alcohols; Animals; Buffers; Calcium Phosphates; Chemical Precipitation; Chromatography, DEAE-Cellulose; Chromatography, Gel; Drug Stability; Electrophoresis; Ethanol; Hydrogen-Ion Concentration; Kinetics; Liver; Macaca; Methods; Mixed Function Oxygenases; Phenylalanine; Protamines; Pteridines; Quaternary Ammonium Compounds; Sulfates; Sulfhydryl Reagents; Sulfur; Sulfuric Acids

1971
Ring-modified substrates of adenosine deaminases.
    Biochemistry, 1969, Volume: 8, Issue:6

    Topics: Adenine; Aminohydrolases; Animals; Aspergillus; Cattle; Chemical Phenomena; Chemistry; Duodenum; Electron Transport; Intestines; Kinetics; Nucleosides; Oxygen; Pteridines; Pyrimidines; Ribose; Sulfur; Thiazoles

1969
Defective molybdopterin biosynthesis: clinical heterogeneity associated with molybdenum cofactor deficiency.
    Journal of inherited metabolic disease, 1995, Volume: 18, Issue:3

    Topics: Adult; Coenzymes; Humans; Male; Metalloproteins; Molybdenum; Molybdenum Cofactors; Pteridines; Purine-Pyrimidine Metabolism, Inborn Errors; Purines; Radiography; Spine; Sulfur

1995
Purification and characterization of a benzylviologen-linked, tungsten-containing aldehyde oxidoreductase from Desulfovibrio gigas.
    Journal of bacteriology, 1995, Volume: 177, Issue:21

    Topics: Aldehyde Oxidoreductases; Amino Acid Sequence; Anaerobiosis; Benzyl Viologen; Coenzymes; Desulfovibrio; Electron Spin Resonance Spectroscopy; Electron Transport; Enzyme Inhibitors; Metalloproteins; Molecular Sequence Data; Molecular Weight; Molybdenum; Molybdenum Cofactors; Protein Conformation; Pteridines; Sequence Analysis; Spectrometry, Fluorescence; Substrate Specificity; Sulfur; Tungsten

1995
Structural characterization of a molybdopterin precursor.
    The Journal of biological chemistry, 1993, Jun-25, Volume: 268, Issue:18

    Topics: Borohydrides; Chromatography, High Pressure Liquid; Coenzymes; Escherichia coli; Magnetic Resonance Spectroscopy; Mass Spectrometry; Metalloproteins; Molybdenum Cofactors; Organophosphorus Compounds; Oxidation-Reduction; Protein Conformation; Protein Precursors; Pteridines; Spectrophotometry, Ultraviolet; Sulfur

1993
In vitro synthesis of molybdopterin from precursor Z using purified converting factor. Role of protein-bound sulfur in formation of the dithiolene.
    The Journal of biological chemistry, 1993, Jun-25, Volume: 268, Issue:18

    Topics: Bacterial Proteins; Chromatography, High Pressure Liquid; Coenzymes; Escherichia coli; Metalloproteins; Molybdenum Cofactors; Organophosphorus Compounds; Protein Precursors; Pteridines; Sulfur; Sulfurtransferases

1993
Characterization by electron paramagnetic resonance of the role of the Escherichia coli nitrate reductase (NarGHI) iron-sulfur clusters in electron transfer to nitrate and identification of a semiquinone radical intermediate.
    Journal of bacteriology, 1997, Volume: 179, Issue:16

    Topics: Benzoquinones; Cell Membrane; Coenzymes; Electron Spin Resonance Spectroscopy; Electron Transport; Escherichia coli; Hydroquinones; Hydroxyquinolines; Iron; Metalloproteins; Molybdenum Cofactors; Mutagenesis, Site-Directed; Nitrate Reductase; Nitrate Reductases; Nitrates; Oxidation-Reduction; Pteridines; Sulfur

1997
Physiological and genetic analyses leading to identification of a biochemical role for the moeA (molybdate metabolism) gene product in Escherichia coli.
    Journal of bacteriology, 1998, Volume: 180, Issue:6

    Topics: Bacterial Proteins; Chlorates; Cloning, Molecular; Coenzymes; DNA, Bacterial; Escherichia coli; Escherichia coli Proteins; Formate Dehydrogenases; Genetic Complementation Test; Glucose; Hydrogen Sulfide; Hydrogenase; Metalloproteins; Methyltransferases; Molybdenum; Molybdenum Cofactors; Multienzyme Complexes; Nitrate Reductase; Nitrate Reductases; Plasmids; Pteridines; Restriction Mapping; Sequence Deletion; Sulfates; Sulfides; Sulfotransferases; Sulfur; Sulfurtransferases

1998
Selenium-containing formate dehydrogenase H from Escherichia coli: a molybdopterin enzyme that catalyzes formate oxidation without oxygen transfer.
    Biochemistry, 1998, Mar-10, Volume: 37, Issue:10

    Topics: Binding Sites; Carbon Dioxide; Catalysis; Coenzymes; Electron Spin Resonance Spectroscopy; Escherichia coli; Formate Dehydrogenases; Formates; Hydrogenase; Iron; Metalloproteins; Molybdenum Cofactors; Multienzyme Complexes; Mutation; Oxidation-Reduction; Oxygen; Photochemistry; Protons; Pteridines; Selenium; Sulfur; Thermodynamics

1998
Molybdopterin radical in bacterial aldehyde dehydrogenases.
    Biochemistry, 1998, Aug-11, Volume: 37, Issue:32

    Topics: Actinobacteria; Aldehyde Dehydrogenase; Bacterial Proteins; Catalysis; Coenzymes; Electron Spin Resonance Spectroscopy; Electron Transport; Gram-Negative Aerobic Rods and Cocci; Iron; Metalloproteins; Molybdenum Cofactors; Oxidation-Reduction; Pteridines; Sulfur

1998
Role of XDHC in Molybdenum cofactor insertion into xanthine dehydrogenase of Rhodobacter capsulatus.
    Journal of bacteriology, 1999, Volume: 181, Issue:9

    Topics: Coenzymes; Enzyme Stability; Flavin-Adenine Dinucleotide; Genes, Bacterial; Iron; Metalloproteins; Models, Biological; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Mutagenesis, Insertional; Open Reading Frames; Pteridines; Rhodobacter capsulatus; Spectrometry, Fluorescence; Spectrophotometry; Sulfur; Transcription, Genetic; Xanthine Dehydrogenase

1999
Purification and characterization of dissimilatory nitrate reductase from a denitrifying halophilic archaeon, Haloarcula marismortui.
    FEBS letters, 2000, Mar-24, Volume: 470, Issue:2

    Topics: Bacteria; Catalysis; Chlorates; Coenzymes; Electron Spin Resonance Spectroscopy; Enzyme Activation; Enzyme Stability; Haloarcula marismortui; Iron; Metalloproteins; Molecular Weight; Molybdenum; Molybdenum Cofactors; Nitrate Reductase; Nitrate Reductases; Nitrates; Nitrites; Oxidation-Reduction; Protein Structure, Quaternary; Pteridines; Sodium Chloride; Sulfur; Thermodynamics

2000
Comparison of the sequences of the Aspergillus nidulans hxB and Drosophila melanogaster ma-l genes with nifS from Azotobacter vinelandii suggests a mechanism for the insertion of the terminal sulphur atom in the molybdopterin cofactor.
    Molecular microbiology, 2000, Volume: 38, Issue:1

    Topics: Amino Acid Sequence; Animals; Aspergillus nidulans; Azotobacter vinelandii; Bacterial Proteins; Cloning, Molecular; Coenzymes; Drosophila melanogaster; Genes, Bacterial; Genes, Fungal; Metalloproteins; Molecular Sequence Data; Molybdenum Cofactors; Pteridines; Sequence Homology, Amino Acid; Sulfur

2000
Identification and biochemical characterization of Arabidopsis thaliana sulfite oxidase. A new player in plant sulfur metabolism.
    The Journal of biological chemistry, 2001, Dec-14, Volume: 276, Issue:50

    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
Molybdenum cofactor deficiency associated with Dandy-Walker complex.
    Brain & development, 2001, Volume: 23, Issue:8

    Topics: Brain; Brain Diseases, Metabolic, Inborn; Coenzymes; Dandy-Walker Syndrome; Humans; Infant, Newborn; Magnetic Resonance Imaging; Male; Metalloproteins; Molybdenum Cofactors; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Sulfur Compounds; Uric Acid; Xanthine Dehydrogenase; Xanthines

2001
New insights into the neuropathogenesis of molybdenum cofactor deficiency.
    The Canadian journal of neurological sciences. Le journal canadien des sciences neurologiques, 2002, Volume: 29, Issue:1

    Topics: Autopsy; Coenzymes; Humans; Immunohistochemistry; Infant; Magnesium; Male; Metalloproteins; Molybdenum Cofactors; Neurodegenerative Diseases; Oxidoreductases Acting on Sulfur Group Donors; Pteridines; Spectrometry, X-Ray Emission; Sulfur

2002
The absence of molybdenum cofactor sulfuration is the primary cause of the flacca phenotype in tomato plants.
    The Plant journal : for cell and molecular biology, 2002, Volume: 31, Issue:3

    Topics: Abscisic Acid; Amino Acid Sequence; Arabidopsis Proteins; Base Sequence; Coenzymes; Genes, Plant; Genetic Complementation Test; Metalloproteins; Molecular Sequence Data; Molybdenum Cofactors; Mutation; Phenotype; Phylogeny; Pteridines; Sequence Alignment; Solanum lycopersicum; Sulfur; Sulfurtransferases

2002
Catalysis at a dinuclear [CuSMo(==O)OH] cluster in a CO dehydrogenase resolved at 1.1-A resolution.
    Proceedings of the National Academy of Sciences of the United States of America, 2002, Dec-10, Volume: 99, Issue:25

    Topics: Aldehyde Oxidoreductases; Alphaproteobacteria; Bacterial Proteins; Binding Sites; Catalysis; Coenzymes; Copper; Electron Spin Resonance Spectroscopy; Enzyme Inhibitors; Metalloproteins; Models, Molecular; Molybdenum; Molybdenum Cofactors; Multienzyme Complexes; Nitriles; Oxidation-Reduction; Potassium Cyanide; Pteridines; Selenium; Structure-Activity Relationship; Sulfur

2002
Synthesis of a molecular Mo2Fe6S9 cluster with the topology of the PN cluster of nitrogenase by rearrangement of an edge-bridged Mo2Fe6S8 double cubane.
    Journal of the American Chemical Society, 2003, Apr-02, Volume: 125, Issue:13

    Topics: Biomimetic Materials; Coenzymes; Crystallography, X-Ray; Iron; Magnetic Resonance Spectroscopy; Metalloproteins; Models, Molecular; Molecular Structure; Molybdenum; Molybdenum Cofactors; Nitrogenase; Organometallic Compounds; Pteridines; Selenium Compounds; Sulfur

2003
The tetrahydropyranopterin structure of the sulfur-free and metal-free molybdenum cofactor precursor.
    The Journal of biological chemistry, 2004, Apr-16, Volume: 279, Issue:16

    Topics: Coenzymes; Escherichia coli; Metalloproteins; Molybdenum; Molybdenum Cofactors; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Pteridines; Sulfur

2004
An evaluation by density functional theory of M-M interactions in organometallic clusters with the [Fe(3)MoS(3)](2+) cores.
    Inorganic chemistry, 2004, May-17, Volume: 43, Issue:10

    Topics: Catechols; Chlorides; Cluster Analysis; Cobalt; Crystallography, X-Ray; Electrons; Iron; Ligands; Models, Molecular; Molybdenum; Nitrogenase; Organometallic Compounds; Oxidation-Reduction; Pteridines; Pyridines; Sulfur

2004
Structure of the molybdopterin-bound Cnx1G domain links molybdenum and copper metabolism.
    Nature, 2004, Aug-12, Volume: 430, Issue:7001

    Topics: Adenosine Monophosphate; Arabidopsis Proteins; Binding Sites; Calnexin; Coenzymes; Copper; Crystallization; Crystallography, X-Ray; Magnesium; Metalloproteins; Models, Molecular; Molybdenum; Molybdenum Cofactors; Plant Proteins; Plants; Protein Binding; Protein Structure, Tertiary; Pteridines; Sulfur

2004
Geometrical control of the active site electronic structure of pyranopterin enzymes by metal-dithiolate folding: aldehyde oxidase.
    Journal of the American Chemical Society, 2004, Sep-29, Volume: 126, Issue:38

    Topics: Aldehyde Oxidase; Binding Sites; Coenzymes; Metalloproteins; Models, Molecular; Molybdenum; Molybdenum Cofactors; Organometallic Compounds; Protein Folding; Pteridines; Structure-Activity Relationship; Sulfur Compounds

2004
In vitro molybdenum ligation to molybdopterin using purified components.
    The Journal of biological chemistry, 2005, Mar-04, Volume: 280, Issue:9

    Topics: Adenosine Triphosphate; Biochemistry; Coenzymes; Dose-Response Relationship, Drug; Escherichia coli; Escherichia coli Proteins; Humans; Magnesium; Metalloproteins; Molybdenum; Molybdenum Cofactors; Organometallic Compounds; Oxidoreductases; Protein Binding; Protein Structure, Tertiary; Pteridines; Pterins; Sulfates; Sulfur; Sulfurtransferases; Time Factors; Tungsten

2005
Molecular characterization of human xanthine oxidoreductase: the enzyme is grossly deficient in molybdenum and substantially deficient in iron-sulphur centres.
    The Biochemical journal, 2005, Jun-01, Volume: 388, Issue:Pt 2

    Topics: Animals; Cattle; Coenzymes; Female; Humans; Iron; Metalloproteins; Milk; Molybdenum; Molybdenum Cofactors; Organometallic Compounds; Pteridines; Spectrum Analysis; Sulfur; Xanthine Dehydrogenase

2005
The nature and function of the catalytic centres of the DMSO reductases.
    Dalton transactions (Cambridge, England : 2003), 2005, Nov-07, Issue:21

    Topics: Binding Sites; Catalysis; Catalytic Domain; Coenzymes; Iron-Sulfur Proteins; Metalloproteins; Models, Molecular; Molecular Conformation; Molybdenum Cofactors; Oxidoreductases; Pteridines; Sulfur

2005
Identification of a Rhodobacter capsulatus L-cysteine desulfurase that sulfurates the molybdenum cofactor when bound to XdhC and before its insertion into xanthine dehydrogenase.
    Biochemistry, 2007, Aug-21, Volume: 46, Issue:33

    Topics: Bacterial Proteins; Carbon-Sulfur Lyases; Coenzymes; Genome, Bacterial; Genomics; Metalloproteins; Molybdenum Cofactors; Protein Interaction Mapping; Pteridines; Rhodobacter capsulatus; Sulfur; Surface Plasmon Resonance; Two-Hybrid System Techniques; Xanthine Dehydrogenase

2007
Crystal structure of a molybdopterin synthase-precursor Z complex: insight into its sulfur transfer mechanism and its role in molybdenum cofactor deficiency.
    Biochemistry, 2008, Jan-15, Volume: 47, Issue:2

    Topics: Apoproteins; Binding Sites; Catalysis; Cloning, Molecular; Coenzymes; Crystallography, X-Ray; Enzyme Precursors; Metalloproteins; Models, Molecular; Molybdenum Cofactors; Mutant Proteins; Protein Structure, Secondary; Pteridines; Staphylococcus aureus; Substrate Specificity; Sulfur; Sulfurtransferases

2008
The sulfurtransferase activity of Uba4 presents a link between ubiquitin-like protein conjugation and activation of sulfur carrier proteins.
    Biochemistry, 2008, Jun-17, Volume: 47, Issue:24

    Topics: Binding Sites; Carrier Proteins; Cell Line, Tumor; Coenzymes; Dimerization; Evolution, Molecular; Humans; Metalloproteins; Molybdenum Cofactors; Nucleotidyltransferases; Pteridines; Saccharomyces cerevisiae Proteins; Structural Homology, Protein; Sulfur; Sulfurtransferases; Thiosulfate Sulfurtransferase; Ubiquitin; Ubiquitins

2008
A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis.
    The Journal of biological chemistry, 2008, Sep-12, Volume: 283, Issue:37

    Topics: Carbon-Sulfur Lyases; Catalysis; Coenzymes; Cytoplasm; Gene Expression Regulation; Humans; Kinetics; Metalloproteins; Models, Biological; Molybdenum Cofactors; Nucleotidyltransferases; Protein Binding; Protein Structure, Tertiary; Pteridines; Sulfur; Sulfurtransferases; Surface Plasmon Resonance; Thiosulfates

2008
A newly discovered role for iron-sulfur clusters.
    Proceedings of the National Academy of Sciences of the United States of America, 2008, Aug-19, Volume: 105, Issue:33

    Topics: Biological Transport; Coenzymes; Electrons; Iron; Metalloproteins; Molybdenum Cofactors; Pteridines; Sulfur; Transcription Factors

2008
IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coli.
    The Journal of biological chemistry, 2010, Jan-22, Volume: 285, Issue:4

    Topics: Carbon-Sulfur Lyases; Catalytic Domain; Coenzymes; Cysteine; Escherichia coli; Escherichia coli Proteins; Metalloproteins; Molybdenum Cofactors; Nucleotidyltransferases; Protein Binding; Pteridines; Species Specificity; Sulfur; Sulfur Compounds; Sulfurtransferases; Surface Plasmon Resonance

2010
Spectroscopic characterization of the molybdenum cofactor of the sulfane dehydrogenase SoxCD from Paracoccus pantotrophus.
    Inorganic chemistry, 2011, Jan-17, Volume: 50, Issue:2

    Topics: Catalytic Domain; Chlorides; Coenzymes; Electron Spin Resonance Spectroscopy; Hydrogen-Ion Concentration; Ligands; Metalloproteins; Molybdenum Cofactors; Paracoccus pantotrophus; Pteridines; Sulfur

2011
The sulfur carrier protein TusA has a pleiotropic role in Escherichia coli that also affects molybdenum cofactor biosynthesis.
    The Journal of biological chemistry, 2013, Feb-22, Volume: 288, Issue:8

    Topics: Carbon-Sulfur Lyases; Coenzymes; Electrophoresis, Gel, Two-Dimensional; Escherichia coli; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Iron-Sulfur Proteins; Metalloproteins; Models, Biological; Molybdenum Cofactors; Mutation; Oligonucleotide Array Sequence Analysis; Pteridines; RNA, Transfer; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Sulfhydryl Compounds; Sulfides; Sulfur; Surface Plasmon Resonance; Transcription, Genetic

2013
The L-cysteine desulfurase NFS1 is localized in the cytosol where it provides the sulfur for molybdenum cofactor biosynthesis in humans.
    PloS one, 2013, Volume: 8, Issue:4

    Topics: Carbon-Sulfur Lyases; Coenzymes; Cysteine; Cytosol; Fluorescence Resonance Energy Transfer; Green Fluorescent Proteins; HeLa Cells; Humans; Metalloproteins; Microscopy, Fluorescence; Molybdenum Cofactors; Mutant Proteins; Neurospora; Nitrate Reductase; Nucleotidyltransferases; Protein Interaction Mapping; Protein Transport; Pteridines; Recombinant Fusion Proteins; Subcellular Fractions; Sulfur; Sulfurtransferases; Surface Plasmon Resonance

2013
TusA (YhhP) and IscS are required for molybdenum cofactor-dependent base-analog detoxification.
    MicrobiologyOpen, 2013, Volume: 2, Issue:5

    Topics: Adenine; Anaerobiosis; Carbon-Sulfur Lyases; Chlorates; Coenzymes; Cysteine; Escherichia coli; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Metalloproteins; Molybdenum Cofactors; Mutagens; Mutation; Pteridines; Signal Transduction; Sulfur

2013