Nobutaka Fujieda

Summary

Affiliation: Kyoto University
Country: Japan

Publications

  1. ncbi request reprint The silent form of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans
    Nobutaka Fujieda
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo ku, Kyoto, Japan
    Biosci Biotechnol Biochem 73:524-9. 2009
  2. doi request reprint Site-directed mutation at residues near the catalytic site of histamine dehydrogenase from Nocardioides simplex and its effects on substrate inhibition
    Maiko Tsutsumi
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo ku, Kyoto 606 8502, Japan
    J Biochem 147:257-64. 2010
  3. ncbi request reprint Redox properties of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans
    Nobutaka Fujieda
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo ku, Kyoto 606 8502, Japan
    Biochim Biophys Acta 1647:289-96. 2003
  4. ncbi request reprint Production of completely flavinylated histamine dehydrogenase, unique covalently bound flavin, and iron-sulfur cluster-containing enzyme of nocardioides simplex in Escherichia coli, and its properties
    Nobutaka Fujieda
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Japan
    Biosci Biotechnol Biochem 69:2459-62. 2005
  5. ncbi request reprint DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation
    Kenji Inaba
    Institute for Virus Research, Kyoto University, Kyoto 606 8507, Japan
    J Biol Chem 279:6761-8. 2004
  6. ncbi request reprint Thermodynamic redox properties governing the half-reduction characteristics of histamine dehydrogenase from Nocardioides simplex
    Maiko Tsutsumi
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto 606 8502, Japan
    Biosci Biotechnol Biochem 72:786-96. 2008
  7. ncbi request reprint Mediated spectroelectrochemical titration of proteins for redox potential measurements by a separator-less one-compartment bulk electrolysis method
    Seiya Tsujimura
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo, Kyoto 606 8502, Japan
    Anal Biochem 337:325-31. 2005
  8. ncbi request reprint Spectroelectrochemical evaluation of redox potentials of cysteine tryptophylquinone and two hemes c in quinohemoprotein amine dehydrogenase from Paracoccus denitrificans
    Nobutaka Fujieda
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo ku, Kyoto 606 8502, Japan
    Biochemistry 41:13736-43. 2002
  9. ncbi request reprint 6-S-cysteinyl flavin mononucleotide-containing histamine dehydrogenase from Nocardioides simplex: molecular cloning, sequencing, overexpression, and characterization of redox centers of enzyme
    Nobutaka Fujieda
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo ku, Kyoto 606 8502, Japan
    Biochemistry 43:10800-8. 2004

Collaborators

Detail Information

Publications9

  1. ncbi request reprint The silent form of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans
    Nobutaka Fujieda
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo ku, Kyoto, Japan
    Biosci Biotechnol Biochem 73:524-9. 2009
    ..The UV-vis spectral properties of the gamma subunit of hydroxylamine-treated QH-AmDH were identical to those of sQH-AmDH. The hydroxylamine-treated QH-AmDH was also reactivated by butylamine, as in the case of sQH-AmDH...
  2. doi request reprint Site-directed mutation at residues near the catalytic site of histamine dehydrogenase from Nocardioides simplex and its effects on substrate inhibition
    Maiko Tsutsumi
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo ku, Kyoto 606 8502, Japan
    J Biochem 147:257-64. 2010
    ..However, destabilization of the semiquinone form leads to kinetic hindrance due to the uphill single electron transfer from the fully reduced CFMN to the [4Fe-4S] cluster...
  3. ncbi request reprint Redox properties of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans
    Nobutaka Fujieda
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo ku, Kyoto 606 8502, Japan
    Biochim Biophys Acta 1647:289-96. 2003
    ..These properties are in marked contrast with those of MADH, which shows high specificity to amicyanin. These electron transfer kinetics are discussed in terms of thermodynamics and structural property...
  4. ncbi request reprint Production of completely flavinylated histamine dehydrogenase, unique covalently bound flavin, and iron-sulfur cluster-containing enzyme of nocardioides simplex in Escherichia coli, and its properties
    Nobutaka Fujieda
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Japan
    Biosci Biotechnol Biochem 69:2459-62. 2005
    ..The purified recombinant enzyme is almost identical with the native enzyme in view of molecular weight and specific activity, and is stoichiometrically assembled with the three cofactors 6-S-cysteinyl FMN, 4Fe-4S cluster, and ADP...
  5. ncbi request reprint DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation
    Kenji Inaba
    Institute for Virus Research, Kyoto University, Kyoto 606 8507, Japan
    J Biol Chem 279:6761-8. 2004
    ..We propose that the Cys44-induced anomaly in ubiquinone represents its activated state, which drives the DsbB-mediated electron transfer...
  6. ncbi request reprint Thermodynamic redox properties governing the half-reduction characteristics of histamine dehydrogenase from Nocardioides simplex
    Maiko Tsutsumi
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto 606 8502, Japan
    Biosci Biotechnol Biochem 72:786-96. 2008
    ..The bell-type pH dependence of the enzymatic activity is also discussed in terms of the pH dependence of the centers' redox potential...
  7. ncbi request reprint Mediated spectroelectrochemical titration of proteins for redox potential measurements by a separator-less one-compartment bulk electrolysis method
    Seiya Tsujimura
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo, Kyoto 606 8502, Japan
    Anal Biochem 337:325-31. 2005
    ..Low-absorbance protein samples (of low concentrations or small absorption coefficients) and hydrophobic proteins (such as membrane-bound proteins) are acceptable for measurements...
  8. ncbi request reprint Spectroelectrochemical evaluation of redox potentials of cysteine tryptophylquinone and two hemes c in quinohemoprotein amine dehydrogenase from Paracoccus denitrificans
    Nobutaka Fujieda
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo ku, Kyoto 606 8502, Japan
    Biochemistry 41:13736-43. 2002
    ..The gamma subunit adsorbed on a glassy carbon electrode, and gave a direct but quasi-reversible electrochemical signal. Intra- and interprotein electron transfers of QH-AmDH are discussed from thermodynamic and structural points of view...
  9. ncbi request reprint 6-S-cysteinyl flavin mononucleotide-containing histamine dehydrogenase from Nocardioides simplex: molecular cloning, sequencing, overexpression, and characterization of redox centers of enzyme
    Nobutaka Fujieda
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo ku, Kyoto 606 8502, Japan
    Biochemistry 43:10800-8. 2004
    ..The structure modeling study, however, demonstrated that a putative substrate-binding cavity in histamine dehydrogenase is quite distinct from that of trimethylamine dehydrogenase...