| Project/Area Number |
23370052
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Structural biochemistry
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| Research Institution | Osaka University |
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Principal Investigator |
FUKUYAMA Keiichi 大阪大学, 工学(系)研究科(研究院), 教授 (80032283)
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| Co-Investigator(Kenkyū-buntansha) |
UNNO Masaki 茨城大学, 理工学研究科, 教授 (10359549)
WADA Kei 宮崎大学, テニュアトラック推進機構, 助教 (80379304)
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| Co-Investigator(Renkei-kenkyūsha) |
IKEUCHI Masahiko 東京大学, 総合文化研究科, 教授 (20159601)
SUGISHIMA Masakazu 久留米大学, 医学部, 准教授 (30379292)
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| Project Period (FY) |
2011-04-01 – 2014-03-31
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥19,890,000 (Direct Cost: ¥15,300,000、Indirect Cost: ¥4,590,000)
Fiscal Year 2013: ¥5,850,000 (Direct Cost: ¥4,500,000、Indirect Cost: ¥1,350,000)
Fiscal Year 2012: ¥6,110,000 (Direct Cost: ¥4,700,000、Indirect Cost: ¥1,410,000)
Fiscal Year 2011: ¥7,930,000 (Direct Cost: ¥6,100,000、Indirect Cost: ¥1,830,000)
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| Keywords | X線結晶解析 / 中性子結晶解析 / ビリン還元酵素 / シアノバクテリオクロム / シトクロムp450還元酵素 / ヘムオキシゲナーゼ / 反応機構 / 立体構造 / シトクロムP450還元酵素 / X線結晶構造解析 / 中性子構造解析 / ビリン色素 / 光合成色素 / 酵素反応機構 |
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| Research Abstract |
We tried to elucidate the molecular mechanism of PcyA, an enzyme that synthesize bilin pigment, through crystal structures. These studies include analysis of PcyA mutants and neutron crystallography as well as X-ray crystallography. PcyA is characteristic in that it reduces two sites of biliverdin sequentially. When the first step is completed, PcyA switches to the second step. We defined Asp105 and other residues are involved in this reaction. We also determined the protonation state Asp105 and biliverdin, and clarified the molecular mechanisms of the reduction.
We succeeded in crystallization of the full-length cyanobacteriochrome.
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