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A change of the metal-specific active site structure of superoxide dismutase from Porphyromonas gingivalis by the mutation of Gly155Thr.

Research Project

Project/Area Number 16591874
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Functional basic dentistry
Research InstitutionMatsumoto Dental University

Principal Investigator

HIRAOKA B.Yukihiro  Matsumoto Dental University, Graduate School of Oral Medicine, Professor, 大学院・歯学独立研究科, 教授 (20097512)

Co-Investigator(Kenkyū-buntansha) YAMASHITA Teruhito  Institute for Oral Science, Assistant Professor, 総合歯科医学研究所, 講師 (90302893)
奥村 茂樹  松本歯科大学, 歯学部, 助手 (80350825)
Project Period (FY) 2004 – 2005
Project Status Completed (Fiscal Year 2005)
Budget Amount *help
¥3,300,000 (Direct Cost: ¥3,300,000)
Fiscal Year 2005: ¥1,300,000 (Direct Cost: ¥1,300,000)
Fiscal Year 2004: ¥2,000,000 (Direct Cost: ¥2,000,000)
KeywordsReactive oxygen / SOD / cambialistic enzyme / Metallo enzyme / Oxidoreductase / Porphyromanas gingivalis / site-directed mutagenesis / EPR spectrum
Research Abstract

Mn-superoxide dismutases (SODs), Fe-SODs and cambialistic SODs, its include P.gingivalis (P.g.) SOD, have a large degree of sequence homology and X-ray structural similarity. Gly155 of P.g.-SOD is located about 11Å from active metal sites and is mostly conserved in aligned amino acid sequences of Mn-SODs, but is substituted for Thr in most Fe-SODs. In order to clarify the structural bases of the metal-specific activity, we analyzed using high-field electron paramagnetic resonance spectroscopy.
We found that Gly155Thr mutation changes the metal-specific activity drastically from a cambialistic type to close to Fe-specific type. Also the Gly155Thr mutant of P.g.-SOD changed the Mn(II) spectrum so that it closely resembled the spectrum of Mn-substituted Fe SOD from E.coli. It has been concluded that Gly155 had universality as one of the amino acid residue which determines the Mn specific activity and Thr on same position had universality as one of the amino acid residue which determines the Fe specifc activity on SODs.

Report

(3 results)
  • 2005 Annual Research Report   Final Research Report Summary
  • 2004 Annual Research Report
  • Research Products

    (6 results)

All 2006 2004

All Journal Article (6 results)

  • [Journal Article] Effects of Substrate Analogues and pH on Manganese Superoxide Dismutases2006

    • Author(s)
      Tabares, LC. et al.
    • Journal Title

      Biochemistry 45・6

      Pages: 1919-1929

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2005 Final Research Report Summary
  • [Journal Article] Effects of Substrate Analogues and pH on Manganese Superoxide Dismutases2006

    • Author(s)
      Tabares LC, et a].
    • Journal Title

      Biochemistry 45(6)

      Pages: 1919-1929

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2005 Final Research Report Summary
  • [Journal Article] Effects of Substrate Analogues and pH on Manganese Superoxide Dismutases2006

    • Author(s)
      Tabares, LC, et al.
    • Journal Title

      Biochemistry 45巻・6号

      Pages: 1919-1929

    • Related Report
      2005 Annual Research Report
  • [Journal Article] Manganese (II) zero-field interaction in cambialistic and manganese superoxide dismutase and its relationship to the structure of the metal binding site.2004

    • Author(s)
      Sun Un, et al.
    • Journal Title

      J. Amer. Chem. Soc. 126・9

      Pages: 2720-2726

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2005 Final Research Report Summary
  • [Journal Article] Manganese(II) zero-field interaction in cambialistic and manganese superoxide dismutase and its relationship to the structure of the metal binding site.2004

    • Author(s)
      Sun Un, et al.
    • Journal Title

      J Amer Chem Soc 126(9)

      Pages: 2720-2726

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2005 Final Research Report Summary
  • [Journal Article] Manganese(II) zero-field interaction in cambialistic and manganese superoxide dismutase and its relationship to the structure of the metal binding site.2004

    • Author(s)
      Sun Un, et al.
    • Journal Title

      J.Amer.Chem.Soc. 126

      Pages: 2720-2726

    • Related Report
      2004 Annual Research Report

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Published: 2004-04-01   Modified: 2016-04-21  

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