Functional expression of an oxygen-tolerant hydrogenase toward mutagenic experiment according to information of the X-ray crystal structure
| Project/Area Number |
25450125
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Applied biochemistry
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| Research Institution | Ibaraki University |
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Principal Investigator |
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2015: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2014: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
Fiscal Year 2013: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | ヒドロゲナーゼ / 水素酸化細菌 / 水素 / 燃料電池触媒 / 蛋白質発現 |
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| Outline of Final Research Achievements |
Heterologous expression of the oxygen-tolerant, highly thermostable membrane-bound hydrogenase from Hydrogenovibrio marinus was performed in Ralstonia eutropha. Expression of the enzyme as a soluble enzyme was also investigated by deletion of the small subunit signal peptide, which is necessary for membrane transduction. However, the result suggested that the process of membrane translocation is necessary for producing a proper conformation possessing high thermal stability. The recombinant enzyme expressed as membrane enzyme exhibited oxygen-tolerance and high thermal stability equivalent to those of the original enzyme. Therefore, the expression system is useful for introducing designed mutations to the H. marinus hydrogenase to study relationship between its unusual properties and structure.
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Report
(4 results)
Research Products
(1 results)
