| Project/Area Number |
19310147
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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 |
Living organism molecular science
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| Research Institution | The Institute of Physical and Chemical Research |
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Principal Investigator |
NAGANO Shingo The Institute of Physical and Chemical Research, 工学研究科, 教授 (60286440)
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| Co-Investigator(Kenkyū-buntansha) |
城 宜嗣 独立行政法人理化学研究所, 城生体金属科学研究室, 主任研究員 (70183051)
松本 悠史 独立行政法人理化学研究所, 城生体金属科学研究室, 協力研究員 (40443030)
平野 聡 独立行政法人理化学研究所, 城生体金属科学研究室, 協力研究員 (10446528)
日野 智也 独立行政法人理化学研究所, 城生体金属科学研究室, 客員研究員 (40373360)
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| Project Period (FY) |
2007 – 2009
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| Project Status |
Completed (Fiscal Year 2009)
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| Budget Amount *help |
¥19,370,000 (Direct Cost: ¥14,900,000、Indirect Cost: ¥4,470,000)
Fiscal Year 2009: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
Fiscal Year 2008: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2007: ¥14,820,000 (Direct Cost: ¥11,400,000、Indirect Cost: ¥3,420,000)
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| Keywords | 呼吸 / 分子進化 / ヘム / 窒素循環 / 呼吸酵素 / 結晶構造 |
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| Research Abstract |
Nitric oxide reductase (NOR) is an iron-containing enzyme that catalyzes the reduction of nitric oxide (NO) to generate a major greenhouse gas, nitrous oxide (N_2O). In this study, we report the crystal structures of cNOR from Pseudomonas aeruginosa at 2.7 angstrom resolution and qNOR from Geobacillus stearothermophilus at 2.5 angstrom resolution. Although the overall structure of these NORs are closely related to cytochrome oxidase (COX), neither the D- nor K-proton pathway, which connect the COX active center to the intracellular space, was observed. Protons required for the cNOR reaction are probably provided from the extracellular side. On the contrary, qNOR has potential proton channel from the cytoplasmic side to the active center.
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