Works matching AU Fujieda, Nobutaka
Results: 16
The Silent Form of Quinohemoprotein Amine Dehydrogenase from Paracoccus denitrificans.
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- Bioscience, Biotechnology & Biochemistry, 2009, v. 73, n. 3, p. 524, doi. 10.1271/bbb.80578
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Thermodynamic Redox Properties Governing the Half-Reduction Characteristics of Histamine Dehydrogenase from Nocardioides simplex.
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- Bioscience, Biotechnology & Biochemistry, 2008, v. 72, n. 3, p. 786, doi. 10.1271/bbb.70665
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Production of Completely Flavinylated Histamine Dehydrogenase, Unique Covalently Bound Flavin, and IronSulfur Cluster-Containing Enzyme of Nocardioides simplex in Escherichia coli, and Its Properties.
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- Bioscience, Biotechnology & Biochemistry, 2005, v. 69, n. 12, p. 2459, doi. 10.1271/bbb.69.2459
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Copper Complexes with Protein‐Based N‐Donor Ligands as cis‐Selective Nascent Cyclopropanases.
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- Chemistry - A European Journal, 2024, v. 30, n. 70, p. 1, doi. 10.1002/chem.202402803
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Copper–Oxygen Dynamics in the Tyrosinase Mechanism.
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- Angewandte Chemie, 2020, v. 132, n. 32, p. 13487, doi. 10.1002/ange.202004733
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Cupin Variants as a Macromolecular Ligand Library for Stereoselective Michael Addition of Nitroalkanes.
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- Angewandte Chemie, 2020, v. 132, n. 20, p. 7791, doi. 10.1002/ange.202000129
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Multifunctions of MelB, a Fungal Tyrosinase from Aspergillus oryzae.
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- ChemBioChem, 2012, v. 13, n. 2, p. 193, doi. 10.1002/cbic.201100609
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Copper(I)-Dioxygen Reactivity in a Sterically Demanding Tripodal Tetradentate tren Ligand: Formation and Reactivity of a Mononuclear Copper(II) End-On Superoxo Complex (Eur. J. Inorg. Chem. 29/2012).
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- European Journal of Inorganic Chemistry, 2012, v. 2012, n. 29, p. n/a, doi. 10.1002/ejic.201290089
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Copper(I)-Dioxygen Reactivity in a Sterically Demanding Tripodal Tetradentate tren Ligand: Formation and Reactivity of a Mononuclear Copper(II) End-On Superoxo Complex.
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- European Journal of Inorganic Chemistry, 2012, v. 2012, n. 29, p. 4574, doi. 10.1002/ejic.201200177
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Heterolytic Alkyl Hydroperoxide O-O Bond Cleavage by Copper(I) Complexes.
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- European Journal of Inorganic Chemistry, 2012, v. 2012, n. 26, p. 4099, doi. 10.1002/ejic.201200555
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Activation mechanism of melB tyrosinase from Aspergillus oryzae by acidic treatment.
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- Journal of Biological Inorganic Chemistry (JBIC), 2013, v. 18, n. 1, p. 19, doi. 10.1007/s00775-012-0945-5
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Tyrosinases in Organic Chemistry: A Versatile Tool for the α-Arylation of β-Dicarbonyl Compounds.
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- European Journal of Organic Chemistry, 2018, v. 2018, n. 15, p. 1789, doi. 10.1002/ejoc.201800188
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Copper–Oxygen Dynamics in the Tyrosinase Mechanism.
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- Angewandte Chemie International Edition, 2020, v. 59, n. 32, p. 13385, doi. 10.1002/anie.202004733
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- Article
Cupin Variants as a Macromolecular Ligand Library for Stereoselective Michael Addition of Nitroalkanes.
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- Angewandte Chemie International Edition, 2020, v. 59, n. 20, p. 7717, doi. 10.1002/anie.202000129
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- Article
Site-directed mutation at residues near the catalytic site of histamine dehydrogenase from Nocardioides simplex and its effects on substrate inhibition.
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- Journal of Biochemistry, 2010, v. 147, n. 2, p. 257, doi. 10.1093/jb/mvp162
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His-Cys and Trp-Cys cross-links generated by post-translational chemical modification.
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- Bioscience, Biotechnology & Biochemistry, 2020, v. 84, n. 3, p. 445, doi. 10.1080/09168451.2019.1696178
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