| Project/Area Number |
60480009
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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 |
植物生理学
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| Research Institution | Tokyo Institute of Technology |
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Principal Investigator |
YAMANAKA Tateo Faculty of Science, Tokyo Institute of Technology, 理学部, 教授 (40028113)
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| Co-Investigator(Kenkyū-buntansha) |
FUKUMORI Yoshihiro Faculty of Science, Tokyo Institute of Technology, 理学部, 助手 (60135655)
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| Project Period (FY) |
1985 – 1986
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| Project Status |
Completed (Fiscal Year 1986)
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| Budget Amount *help |
¥6,900,000 (Direct Cost: ¥6,900,000)
Fiscal Year 1986: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1985: ¥6,200,000 (Direct Cost: ¥6,200,000)
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| Keywords | Iron oxidizing bacteria / Oxidation of ferrous ions Iron oxidizing enzyme / Cytochrome / 電子伝達 / Thiobacillus ferrooxidans |
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| Research Abstract |
This research has been performed to elucidate the molecular mechanisms of the oxidation of ferrous ions by the iron oxidizing bacterium, Thiobacillus ferrooxidans. Cytochrome c-552 and an iron oxidizing enzyme have been purified to an electrophoretically homogeneous state and the electron transport system coupled with the oxidation of ferrous ions has been inferred.
Cytochrome c-552 shows absorption peak at 411 nm in the oxidized form and peaks at 417, 523 and 552 nm in the reduced form. Its molecular weight is 14,000 and its reduced form is oxidized by a membrane-bound a-type cytochrome of the organism. The iron oxidizing enzyme showed absorption peaks at 282 and 382 nm. The enzyme has 18-20 atoms of nonhaem iron and 6 atoms of acid labile sulphur in the molecule and its molecular weight is 63,000. It catalyses rapid reduction of rusticyanin ( a copper protein ) in the presence of ferrous ions. The electron transport coupled with the oxidation of ferrous ions in the bacterium is inferred as follows:
<Fe^(2+)> ->Iron oxidizing enzyme->Rusticyanin->Cytochrome c-552->a-Type cytochrome-> <O_2> The electron transport system coupled with the oxidation of ferrous ions will be completely reconstituted with the purified components by future studies.
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