| Project/Area Number |
03453084
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
工業物理化学・複合材料
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| Research Institution | Tokyo Institute of Technology |
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Principal Investigator |
OKURA Ichiro Tokyo Institute of Technology, Department of Bioengineering, Professor, 生命理工学部, 教授 (90089821)
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| Co-Investigator(Kenkyū-buntansha) |
AONO Shigetoshi Tokyo Institute of Technology, Department of Bioengineering, Research Associate, 生命理工学部, 助手 (60183729)
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| Project Period (FY) |
1991 – 1993
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| Project Status |
Completed (Fiscal Year 1993)
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| Budget Amount *help |
¥6,600,000 (Direct Cost: ¥6,600,000)
Fiscal Year 1993: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1992: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 1991: ¥4,500,000 (Direct Cost: ¥4,500,000)
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| Keywords | Thermophilic Hydrogen / Hydrogenase / Ferredoxin Oxidizing Bacterium / Iron-Sulfur Cluster / 水素発生反応 / 好熱性細菌 / ヒドロゲナ-ゼ |
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| Research Abstract |
In this work, we purified a ferredoxin and a hydrogenase from a thermophilic hydrogen oxidizing bacterium, Bacillus schlegelii and studied their biochemical and biophysical properties. The ferredoxin contains one [3Fe-4S] and one [4Fe-4S] cluster in a molecule. The amino acid sequence of the ferredoxin is homologous to other 7Fe type ferredoxin. This ferredoxin is active as an electron transfer agent in a reaction system for the reduction of cytochrome c consisting of NADPH, FNR, and cytochrome c. Only [3Fe-4S] cluster acts as the active site for the electron transfer reaction in the reduction of cytochrome c. This is caused by too low redox potential of the [4Fe-4S] cluster to be reduced in the reaction system.
The hydrogenase purified from the bacterium is an up-take type hydrogenase that catalyzes the oxidation of hydrogen predominantly. This hydrogenase possesses 50% of the initial activity after 5 and 2.5 hours of heat treatment at 70 and 80ﾟC, respectively showing is very thermostable.
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