Structure of Substrate-bound Nitric Oxide Reductases
Project/Area Number |
22310137
|
Research Category |
Grant-in-Aid for Scientific Research (B)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Living organism molecular science
|
Research Institution | Tottori University |
Principal Investigator |
NAGANO Shingo 鳥取大学, 大学院・工学研究科, 教授 (60286440)
|
Project Period (FY) |
2010 – 2012
|
Project Status |
Completed (Fiscal Year 2012)
|
Budget Amount *help |
¥19,890,000 (Direct Cost: ¥15,300,000、Indirect Cost: ¥4,590,000)
Fiscal Year 2012: ¥5,720,000 (Direct Cost: ¥4,400,000、Indirect Cost: ¥1,320,000)
Fiscal Year 2011: ¥5,720,000 (Direct Cost: ¥4,400,000、Indirect Cost: ¥1,320,000)
Fiscal Year 2010: ¥8,450,000 (Direct Cost: ¥6,500,000、Indirect Cost: ¥1,950,000)
|
Keywords | 呼吸 / 分子進化 / ヘム / 窒素循環 / 呼吸酵素 / 結晶構造 |
Research Abstract |
The structures of quinol and cytochrome c-dependent nitric oxide reductases, which catalyze the reduction of NO to produce N2O, has been characterized. The structure-based mutagenesis and molecular dynamics simulation studies of qNOR suggest that a water channel from the cytoplasm can serve as a proton transfer pathway for the catalytic reaction. Further structural comparison of qNOR with cNOR and aerobic and microaerobic respiratory oxidases elucidates their evolutionary relationship and possible functional conversions.
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Report
(4 results)
Research Products
(29 results)