Quinoprotein-dependent periplasmic oxidase system in aerobic bacteria
Grant-in-Aid for International Scientific Research.
|Allocation Type||Single-year Grants|
|Research Institution||Yamaguchi University|
ADACHI Osao Faculty of Agriculture, Yamaguchi University, Professor, 農学部, 教授 (20027189)
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 Fiscal Year
Completed(Fiscal Year 1995)
|Keywords||Pyrroloquinoline quinone / Quinoprotein / Electron transport chain / Periplasmic oxidase|
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.
Research Output (8results)