2012 Fiscal Year Final Research Report
Structure of Substrate-bound Nitric Oxide Reductases
| Project/Area Number |
22310137
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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 | Tottori University |
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Principal Investigator |
NAGANO Shingo 鳥取大学, 大学院・工学研究科, 教授 (60286440)
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| Project Period (FY) |
2010 – 2012
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| Keywords | 呼吸 / 分子進化 / ヘム / 窒素循環 |
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| 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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[Journal Article] Crystal structure of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus2012
Author(s)
Matsumoto, Y., Tosha, T., Pisliakov, A. V., Hino, T., Sugimoto, H., *Nagano, S.(2) *, Sugita, Y., and *Shiro, Y.
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Journal Title
Nature Struct. Mol. Biol
Volume: 19
Pages: 238-245
DOI
Peer Reviewed
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