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Quinoprotein-dependent periplasmic oxidase system in aerobic bacteria

Research Project

Project/Area Number 07044324
Research Category

Grant-in-Aid for International Scientific Research.

Allocation TypeSingle-year Grants
Research InstitutionYamaguchi University

Principal Investigator

ADACHI Osao  Faculty of Agriculture, Yamaguchi University, Professor, 農学部, 教授 (20027189)

Co-Investigator(Kenkyū-buntansha) ヨハネス ダイナ  デルフト工科大学, 生物工学部, 教授
アーノルド シュワルツ  ボン大学, 植物学研究所, 教授
ヘルムート ゲオリッシュ  ベルリン工科大学, 生物工学研究所, 教授
SHINAGAWA Emiko  Faculty of Biotechnology, Ube Technical College, Associate Professor, 生物工学科, 助教授 (20116726)
TOYAMA Hirohide  Faculty of Agriculture, Yamaguchi University, Research Associate, 農学部, 助手 (60240884)
YAMADA Mamoru  Faculty of Agriculture, Yamaguchi University, Associate Professor, 農学部, 助教授 (30174741)
MATSUSHITA Kazunobu  Faculty of Agriculture, Yamaguchi University, Professor, 農学部, 教授 (50107736)
DUINE A.johannis  Faculty of Engineering, Delft University of Technology, Professor
SCHWARTZ C.arnold  Institute of Botany, University of Bonn, Professor
GOERISCH Helmut  Institute of Biotechnology, Berlin Technical University, Professor
Project Period (FY) 1995
Project Status Completed (Fiscal Year 1995)
KeywordsPyrroloquinoline quinone / Quinoprotein / Electron transport chain / Periplasmic oxidase
Research Abstract

One year collaboration with three different institutes from Germany and the Netherlands has yielded the following results.
(1) A novel bacterial strain, Pseudomonas putida HK5, was isolated from soil by enrichment technique. Three distinct quinoprotein alcohol dehydrogenases are expressed when grown on different alcohols. They are one quinoprotein and two quinohemoproteins and they showed interesting aspects in biochemistry, physiology and applied enzymology, on the basis of periplasmic oxidase.
(2) Glucose dehydrogenase, a typical quinoprotein, is divided into two species depending on their localization, membrane-bound and soluble enzymes. The two enzymes were highly purified and converted to the apo-enzymes. The binding process of PQQ to the apo-enzymes was investigated revealing that the two enzymes are completely different each other in many aspects.
(3) An inactive enzyme of alcohol dehydrogenase has been purified from the membrane fraction of Gluconobacter suboxydans. It is interesting very much to know that the inactive enzyme can be converted to the active one by the expenses of biological energy.
(4) Alcohol dehydrogenase from Gluconobacter suboxydans is consisted of three different subunits. The second subunit contains three moles of cytochromes c and shows an interesting phenomena during the catalytic activity of alcohol oxidation. Several evidence for intramolecular flow of electron during enzyme activity were presented for the first time.

Report

(1 results)
  • 1995 Final Research Report Summary
  • Research Products

    (8 results)

All Other

All Publications (8 results)

  • [Publications] 外山博英ら: "Three Distinct Quinoprotein Alcohol Dehydrogenases are Expressed when Pseudomonas Putda is Grown on Different Alcohols" J.Bacteriology. 177. 2442-2450 (1995)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] 松下一信ら: "Soluble and Membrane-Bound Quinoprotein D-Glucose Dehydrogenases of The Acinetobacter-Calcoaceticus - The Binding Process of PQQ to The Apoenzymes" Biosci.biotech.Bio Chem.59. 1548-1555 (1995)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] 松下一信ら: "Generation Mechanism and Purification of an Inactive From Convertible In-Vivo to The Active From of Quinoprotein Alcohol-Dehydrogenase in Gluconobacter Suboxydans" J.Bacteriologs. 177. 6552-6559 (1995)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] 松下一信ら: "Function of Muliple here C Moieties in Intramolecular Electron Transport and Ubiquinone Reduction in The Quinohemoprotein Alcohol Dehydrogenase Cytochrome C Complex of Gluconobacter Suboxydans" J.Biol.Chem. 271. (1996)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] H.Toyama et al.: "Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols" J.Bacteriology. 177. 2442-2450 (1995)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] K.Matsushita et al.: "Soluble and membrane-bound quinoprotein glucose dehydrogenases of the Acinetobacter calcoaceticus : The binding process of PQQ to the apoenzymes" Biosci.Biotech.Biochem.59. 1548-1555 (1995)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] K.Matsushita et al.: "Generation mechanism and purification of an inactive form convertibleto the active form of quinoprotein alcohol dehydrogenase in Gluconobacter suboxydans" J.Bacteriology. 177. 6552-6559 (1995)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] K.Matsushita et al.: "Function of multiple heme c moieties in intramolecular electron transport and ubiquinone reduction in quinoprotein alcohol dehydrogenase-cytochrome c complex of Gluconobacter suboxydans" J.Biol.Chem.271. Febrary issue (1996)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1995 Final Research Report Summary

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Published: 1997-03-04   Modified: 2016-04-21  

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