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2007 Fiscal Year Final Research Report Summary

The occurrence of a new yellow enzyme in Gluconobacter strains

Research Project

Project/Area Number 18580084
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Applied microbiology
Research InstitutionUbe National College of Technology

Principal Investigator

SHINAGAWA Emiko  Ube National College of Technology, Department of Chemical and Biological Engineering, Professor (20116726)

Project Period (FY) 2006 – 2007
Keywordsold yellow enzyme / acetic acid bacteria / oxidative fermentation / new yellow enzyme / NADH dehydrogenase / NADPH dehvdrogenase
Research Abstract

A new yellow enzyme, distinct from an old yellow enzyme, was found in the same cytoplasmic fraction of Gluconobacter strains. A new yellow enzyme and an old yellow enzyme were purified from the cytoplasm of G. oxydans IFO 3244. These two enzymes were purified and crystallized. While an old yellow enzyme is NADPH dehydrogenase catalyzing the oxidation of NADPH to NADP, a new yellow enzyme was hind to be NADH dehydrogenase oxidizing NADH to NAD. Molecular mass of NADH dehydrogenase and NADPH dehydrogenase was estimated to be 120kDa and 50-60kDa, respectively. The former enzyme was consisted of four identical subunits with 301cDa and the molecular mass of subunit of the latter enzyme was 50kDa. The absorption spectra of NADH dehydrogenase showed two absorption maxima in the visible region at 445 and 340nm, with clear shoulders at 468 and 420nm, and NADPH dehydrogenase also showed two absorption maxima in the visible region, at 470 and 377 nm, with slight shoulders at 490 and 450nm. The ab … More sorption spectrum of these two enzymes was reduced by the addition of each substrate, NADH and NADPH, and the spectrum of NADH-or NADPH-reduced enzyme was restored to the original level after the enzyme solution was bubbled with oxygen. FAD and FMN were identified as the coenzyme of NADH dehydrogenase and NADPH dehydrogenase, respectively. The oxidation rate of NADH to NADPH with NADH dehydrogenase gave 3.0, and that of NADPH to NADH with NADPH dehydrogenase gave 2.0. The reaction rate by NADH dehydrogenase and also NADPH dehydrogenase was relatively low when molecular oxygen was used as the electron acceptor. The artificial electron acceptors such as p-benzoquinone and 2, 6-clichlorophenolindophenol were more effective electron acceptors than molecular oxygen for both enzymes. The N-terminal amino acid sequence of NADH dehydrogenase showed 100% similarity with a non-heme chloroperoxidase and that of NADPH dehydrogenase matched 100% a putative oxidoreductase containing the old yellow enzyme-like FMN-binding domains. NADH dehydrogenase might function to regenerate NAD coupling with NAD-dependent dehydrogenases in cytoplasm of Gluconobacter strains like NADPH dehydrogenase function to regenerate NADP coupling with NADP-dependent dehydrogenases. Less

  • Research Products

    (6 results)

All 2008

All Journal Article (4 results) (of which Peer Reviewed: 2 results) Presentation (2 results)

  • [Journal Article] The occurrence of a novel NADH dehydrogenase,distinct from the old yellow enzyme,in Gluconobacter strains2008

    • Author(s)
      品川 恵美子
    • Journal Title

      Bioscience, Biotechnology, and Biochemistry 72

      Pages: 260-264

    • Description
      「研究成果報告書概要(和文)」より
    • Peer Reviewed
  • [Journal Article] Formaldehyde elimination with formaldehyde and formate oxidase in membrane of acetic acid bacteria2008

    • Author(s)
      品川 恵美子
    • Journal Title

      Journal of Bioscience and Biotechnology 105

      Pages: 292-295

    • Description
      「研究成果報告書概要(和文)」より
    • Peer Reviewed
  • [Journal Article] The occurrence of a novel NADH dehydrogenase, distinct from the old yellow enzyme, in Gluconobacter strains2008

    • Author(s)
      Emiko Shinagawa, Yoshitaka Ano, Osao Adachi, Kazunobu Matsushita
    • Journal Title

      Biosci. Biotechnol. Biochem. 72-1

      Pages: 260-264

    • Description
      「研究成果報告書概要(欧文)」より
  • [Journal Article] Formaldehyde elimination with formaldehyde and formate oxidase in membrane of acetic acid bacteria2008

    • Author(s)
      Emiko Shinagawa, Hirohide Toyama, Kazunobu Matsushita, Pravate Tuitemwrong, Ganjana Theeragool, Osao Adachi
    • Journal Title

      J. Biosci. Bioeng. 105-3

      Pages: 292-295

    • Description
      「研究成果報告書概要(欧文)」より
  • [Presentation] 酢酸菌細胞質に見出された新規なNADH脱水素酵素2008

    • Author(s)
      品川 恵美子
    • Organizer
      日本農芸化学会大会
    • Place of Presentation
      名城大学
    • Year and Date
      2008-03-27
    • Description
      「研究成果報告書概要(和文)」より
  • [Presentation] The occurrence of a novel NADH dehydrogenase in Gluconobacter strains2008

    • Author(s)
      Emiko Shinagawa, Yoshitaka Ano, Osao Adachi, Kazunobu Matsushita
    • Organizer
      2008 Annual Meeting of the Japan Society for Bioscience, Biotechnology, and Agrochemistry
    • Place of Presentation
      Nagoya
    • Year and Date
      2008-03-27
    • Description
      「研究成果報告書概要(欧文)」より

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Published: 2010-02-04  

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