Mechanism of catalytic nitric oxide reduction by membrane-bound nitric oxide reductase : comparison with oxygen reduction reaction
| Project/Area Number |
22770136
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Functional biochemistry
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| Research Institution | The Institute of Physical and Chemical Research |
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Principal Investigator |
TOSHA Takehiko 独立行政法人理化学研究所, 城生体金属科学研究室, 研究員 (00548993)
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| Research Collaborator |
PISLIAKOV Andrei 独立行政法人理化学研究所, 杉田理論生物化学研究室, 基礎科学特別研究員 (70565770)
ADELROTH Pia ストックホルム大学, Department of Biochemistry & Biophysics, 准教授
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| Project Period (FY) |
2010 – 2011
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| Project Status |
Completed (Fiscal Year 2011)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2011: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2010: ¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
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| Keywords | 一酸化窒素 / 金属酵素 / 結晶構造解析 / 生体分子分光 / 膜タンパク質 / プロトンポンプ / ヘム / 呼吸酵素 / 一酸化窒素還元酵素 / 呼吸鎖末端酸化酵素 / X線結晶構造解析 / 共鳴ラマン分光 / 酵素反応機構 / 膜蛋白質 / 反応中間体 |
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| Research Abstract |
Structures of reduced and CN-bound oxidized nitric oxide reductase(NOR), which is involved in anaerobic respiration chain, were determined by X-ray crystallography. Resonance Raman measurement indicated that the substrate, NO, bound to the active site heme in a bent conformation. The proton transfer mechanism was also examined by molecular dynamics simulation, suggesting the structural factor(s) controlling the catalytic proton transfer in NOR. These findings help us understanding the molecular mechanism of the NO reduction reaction in NOR and the functional conversion from NOR to aerobic respiration enzyme during the molecular evolution.
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Report
(3 results)
Research Products
(34 results)
