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Role of Conductive Nanoparticles in the Direct Unmediated Bioelectrocatalysis of Immobilized Sulfite Oxidase.
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- Electroanalysis, 2016, v. 28, n. 10, p. 2303, doi. 10.1002/elan.201600246
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A pH Responsive Redox Hydrogel for Electrochemical Detection of Redox Silent Biocatalytic Processes. Control of Hydrogel Solvation.
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- Electroanalysis, 2015, v. 27, n. 4, p. 938, doi. 10.1002/elan.201400621
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- Article
A Biosensor for Aromatic Aldehydes Comprising the Mediator Dependent PaoABC-Aldehyde Oxidoreductase.
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- Electroanalysis, 2013, v. 25, n. 1, p. 101, doi. 10.1002/elan.201200362
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- Article
Hohe elektromagnetische Feldverstärkung in nanotubularen TiO<sub>2</sub>‐Elektroden.
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- Angewandte Chemie, 2018, v. 130, n. 24, p. 7344, doi. 10.1002/ange.201802597
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- Article
Strukturelle Einblicke in den Mo-Cofaktor-Einbau in Sulfitoxidase durch ortsspezifische Spinmarkierung.
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- Angewandte Chemie, 2015, v. 127, n. 40, p. 12033, doi. 10.1002/ange.201504772
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- Article
Tellurite resistance gene trgB confers copper tolerance to Rhodobacter capsulatus.
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- BioMetals, 2012, v. 25, n. 5, p. 995, doi. 10.1007/s10534-012-9566-2
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- Article
Ten novel mutations in the molybdenum cofactor genes MOCS1 and MOCS2 and in vitro characterization of a MOCS2 mutation that abolishes the binding ability of molybdopterin synthase.
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- Human Genetics, 2005, v. 117, n. 6, p. 565, doi. 10.1007/s00439-005-1341-9
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- Article
Same but different: Comparison of two system-specific molecular chaperones for the maturation of formate dehydrogenases.
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- PLoS ONE, 2018, v. 13, n. 11, p. 1, doi. 10.1371/journal.pone.0201935
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Direct comparison of the four aldehyde oxidase enzymes present in mouse gives insight into their substrate specificities.
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- PLoS ONE, 2018, v. 13, n. 1, p. 1, doi. 10.1371/journal.pone.0191819
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The chaperone FdsC for Rhodobacter capsulatus formate dehydrogenase binds the bis-molybdopterin guanine dinucleotide cofactor.
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- FEBS Letters, 2014, v. 588, n. 4, p. 531, doi. 10.1016/j.febslet.2013.12.033
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Role of Human Aldehyde Oxidase in the Generation of Reactive Oxygen Species during the Metabolism of Nicotine.
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- FASEB Journal, 2022, v. 36, p. N.PAG, doi. 10.1096/fasebj.2022.36.S1.L7796
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- Article
The Mechanism of Metal-Containing Formate Dehydrogenases Revisited: The Formation of Bicarbonate as Product Intermediate Provides Evidence for an Oxygen Atom Transfer Mechanism.
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- Molecules, 2023, v. 28, n. 4, p. 1537, doi. 10.3390/molecules28041537
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- Article
The Role of the Nucleotides in the Insertion of the bis-Molybdopterin Guanine Dinucleotide Cofactor into apo-Molybdoenzymes.
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- Molecules, 2022, v. 27, n. 9, p. 2993, doi. 10.3390/molecules27092993
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- Article
Mutations in LYRM4, encoding iron–sulfur cluster biogenesis factor ISD11, cause deficiency of multiple respiratory chain complexes.
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- Human Molecular Genetics, 2013, v. 22, n. 22, p. 4460, doi. 10.1093/hmg/ddt295
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A Minimal Light‐Driven System to Study the Enzymatic CO<sub>2</sub> Reduction of Formate Dehydrogenase.
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- ChemCatChem, 2022, v. 14, n. 24, p. 1, doi. 10.1002/cctc.202201067
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Changing the Electron Acceptor Specificity of Rhodobacter capsulatus Formate Dehydrogenase from NAD + to NADP +.
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- International Journal of Molecular Sciences, 2023, v. 24, n. 22, p. 16067, doi. 10.3390/ijms242216067
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Structural Data on the Periplasmic Aldehyde Oxidoreductase PaoABC from Escherichia coli: SAXS and Preliminary X-ray Crystallography Analysis.
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- International Journal of Molecular Sciences, 2014, v. 15, n. 2, p. 2223, doi. 10.3390/ijms15022223
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The [4Fe‐4S]‐Cluster of HydF is not Required for the Binding and Transfer of the Diiron Site of [FeFe]‐Hydrogenases.
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- ChemBioChem, 2023, v. 24, n. 11, p. 1, doi. 10.1002/cbic.202300222
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The biosynthesis of the molybdenum cofactors.
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- Journal of Biological Inorganic Chemistry (JBIC), 2015, v. 20, n. 2, p. 337, doi. 10.1007/s00775-014-1173-y
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Human aldehyde oxidase (hAOX1): structure determination of the Moco‐free form of the natural variant G1269R and biophysical studies of single nucleotide polymorphisms.
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- FEBS Open Bio, 2019, v. 9, n. 5, p. 925, doi. 10.1002/2211-5463.12617
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High Electromagnetic Field Enhancement of TiO<sub>2</sub> Nanotube Electrodes.
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- Angewandte Chemie International Edition, 2018, v. 57, n. 24, p. 7225, doi. 10.1002/anie.201802597
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- Article
Structural Insights into the Incorporation of the Mo Cofactor into Sulfite Oxidase from Site-Directed Spin Labeling.
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- Angewandte Chemie International Edition, 2015, v. 54, n. 40, p. 11865, doi. 10.1002/anie.201504772
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Crystal structure of YnjE from Escherichia coli, a sulfurtransferase with three rhodanese domains.
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- Protein Science: A Publication of the Protein Society, 2009, v. 18, n. 12, p. 2480, doi. 10.1002/pro.260
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Infrared Spectroscopy Elucidates the Inhibitor Binding Sites in a Metal‐Dependent Formate Dehydrogenase.
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- Chemistry - A European Journal, 2022, v. 28, n. 54, p. 1, doi. 10.1002/chem.202201091
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- Article
The sulfite oxidase Shopper controls neuronal activity by regulating glutamate homeostasis in Drosophila ensheathing glia.
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- Nature Communications, 2018, v. 9, n. 1, p. 1, doi. 10.1038/s41467-018-05645-z
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Iron Sulfur and Molybdenum Cofactor Enzymes Regulate the Drosophila Life Cycle by Controlling Cell Metabolism.
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- Frontiers in Physiology, 2018, p. 1, doi. 10.3389/fphys.2018.00050
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Discovery of the Lanthipeptide Curvocidin and Structural Insights into its Trifunctional Synthetase CuvL.
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- Angewandte Chemie International Edition, 2023, v. 62, n. 23, p. 1, doi. 10.1002/anie.202302490
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The biosynthesis of the molybdenum cofactors in Escherichia coli.
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- Environmental Microbiology, 2020, v. 22, n. 6, p. 2007, doi. 10.1111/1462-2920.15003
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Galactose Oxidase Variants for the Oxidation of Amino Alcohols in Enzyme Cascade Synthesis.
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- ChemCatChem, 2015, v. 7, n. 15, p. 2313, doi. 10.1002/cctc.201500218
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Biochemical, Stabilization and Crystallization Studies on a Molecular Chaperone (PaoD) Involved in the Maturation of Molybdoenzymes.
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- PLoS ONE, 2014, v. 9, n. 1, p. 1, doi. 10.1371/journal.pone.0087295
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Identification of Crucial Amino Acids in Mouse Aldehyde Oxidase 3 That Determine Substrate Specificity.
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- PLoS ONE, 2013, v. 8, n. 12, p. 1, doi. 10.1371/journal.pone.0082285
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The Respiratory Arsenite Oxidase: Structure and the Role of Residues Surrounding the Rieske Cluster.
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- PLoS ONE, 2013, v. 8, n. 8, p. 1, doi. 10.1371/journal.pone.0072535
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The L-Cysteine Desulfurase NFS1 Is Localized in the Cytosol where it Provides the Sulfur for Molybdenum Cofactor Biosynthesis in Humans.
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- PLoS ONE, 2013, v. 8, n. 4, p. 1, doi. 10.1371/journal.pone.0060869
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Novel Frataxin Isoforms May Contribute to the Pathological Mechanism of Friedreich Ataxia.
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- PLoS ONE, 2012, v. 7, n. 10, p. 1, doi. 10.1371/journal.pone.0047847
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Elucidation of the Dual Role of Mycobacterial MoeZR in Molybdenum Cofactor Biosynthesis and Cysteine Biosynthesis.
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- PLoS ONE, 2011, v. 6, n. 11, p. 1, doi. 10.1371/journal.pone.0028170
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Site Directed Mutagenesis of Amino Acid Residues at the Active Site of Mouse Aldehyde Oxidase AOX1.
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- PLoS ONE, 2009, v. 4, n. 4, p. 1, doi. 10.1371/journal.pone.0005348
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Electrocatalytic sulfite biosensor with human sulfite oxidase co-immobilized with cytochrome c in a polyelectrolyte-containing multilayer.
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- Analytical & Bioanalytical Chemistry, 2009, v. 393, n. 1, p. 225, doi. 10.1007/s00216-008-2432-y
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- Article
Structure and function of mammalian aldehyde oxidases.
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- Archives of Toxicology, 2016, v. 90, n. 4, p. 753, doi. 10.1007/s00204-016-1683-1
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- Article
The Human Mercaptopyruvate Sulfurtransferase TUM1 Is Involved in Moco Biosynthesis, Cytosolic tRNA Thiolation and Cellular Bioenergetics in Human Embryonic Kidney Cells.
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- Biomolecules (2218-273X), 2023, v. 13, n. 1, p. 144, doi. 10.3390/biom13010144
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Shared Sulfur Mobilization Routes for tRNA Thiolation and Molybdenum Cofactor Biosynthesis in Prokaryotes and Eukaryotes.
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- Biomolecules (2218-273X), 2017, v. 7, n. 1, p. 5, doi. 10.3390/biom7010005
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Mechanistic insights into the ROS‐mediated inactivation of human aldehyde oxidase.
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- FEBS Letters, 2023, v. 597, n. 13, p. 1792, doi. 10.1002/1873-3468.14669
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A periplasmic aldehyde oxidoreductase represents the first molybdopterin cytosine dinucleotide cofactor containing molybdo-flavoenzyme from Escherichia coli.
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- FEBS Journal, 2009, v. 276, n. 10, p. 2762, doi. 10.1111/j.1742-4658.2009.07000.x
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- Article
Heavy metal ions inhibit molybdoenzyme activity by binding to the dithiolene moiety of molybdopterin in Escherichia coli.
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- FEBS Journal, 2008, v. 275, n. 22, p. 5678, doi. 10.1111/j.1742-4658.2008.06694.x
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- Article
Site-directed mutagenesis of the active site loop of the rhodanese-like domain of the human molybdopterin synthase sulfurase MOCS3.
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- FEBS Journal, 2007, v. 274, n. 11, p. 2778, doi. 10.1111/j.1742-4658.2007.05811.x
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Cover Feature: The 1,6,7,12-Tetraazaperylene Bridging Ligand as an Electron Reservoir and Its Disulfonato Derivative as Redox Mediator in an Enzyme-Electrode Process (Chem. Eur. J. 62/2017).
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- Chemistry - A European Journal, 2017, v. 23, n. 62, p. 15539, doi. 10.1002/chem.201704226
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- Article
The 1,6,7,12-Tetraazaperylene Bridging Ligand as an Electron Reservoir and Its Disulfonato Derivative as Redox Mediator in an Enzyme-Electrode Process.
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- Chemistry - A European Journal, 2017, v. 23, n. 62, p. 15583, doi. 10.1002/chem.201703639
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Metal-Containing Formate Dehydrogenases, a Personal View.
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- Molecules, 2023, v. 28, n. 14, p. 5338, doi. 10.3390/molecules28145338
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- Article
The ABCB7-Like Transporter PexA in Rhodobacter capsulatus Is Involved in the Translocation of Reactive Sulfur Species.
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- Frontiers in Microbiology, 2019, p. N.PAG, doi. 10.3389/fmicb.2019.00406
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Iron‐sulfur cluster carrier proteins involved in the assembly of Escherichia coli NADH:ubiquinone oxidoreductase (complex I).
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- Molecular Microbiology, 2019, v. 111, n. 1, p. 31, doi. 10.1111/mmi.14137
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Electrochemical Trimethylamine N -Oxide Biosensor with Enzyme-Based Oxygen-Scavenging Membrane for Long-Term Operation under Ambient Air.
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- Biosensors (2079-6374), 2021, v. 11, n. 4, p. 98, doi. 10.3390/bios11040098
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- Article