2015 Fiscal Year Final Research Report
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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| 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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| Free Research Field |
応用微生物学
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