2015 Fiscal Year Final Research Report
Structure determination of heme oxygenase bound to its weakly interacted protein
| Project/Area Number |
25840026
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Structural biochemistry
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| Research Institution | Kurume University |
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Principal Investigator |
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| Project Period (FY) |
2013-04-01 – 2016-03-31
|
| Keywords | X線結晶構造解析 / 電子移動 / 酸化還元複合体 |
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| Outline of Final Research Achievements |
Heme oxygenase (HO) is the major enzyme involved in heme degradation utilizing the redox equivalents supplied from NADPH-cytochrome P450 reductase (CPR). In this study, we found that the mutated CPR (ΔTGEE) is strongly interacted with heme-HO complex. We could determine the crystal structure of ΔTGEE-heme-HO complex at 4.3Å resolution. Based on the structure, the mechanism of the electron transfer from CPR to heme-HO complex accompanied with the large domain motion of CPR has been proposed. The proposed mechanism of the electron transfer was supported by the results from small-angle X-ray scattering, cross-linking, and ultra-centrifuge techniques.
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| Free Research Field |
構造生物学
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