| Project/Area Number |
19510224
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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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 | Rikkyo University |
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Principal Investigator |
MAKINO Ryu Rikkyo University, 理学部, 教授 (40101026)
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| Co-Investigator(Renkei-kenkyūsha) |
SHIRO Yoshitugu 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)
PAKU Sanyou 横浜市立大学, 国際総合科学研究科, 准教授 (20291932)
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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 |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2009: ¥650,000 (Direct Cost: ¥500,000、Indirect Cost: ¥150,000)
Fiscal Year 2008: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2007: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | 活性発現の分子機構 / 可溶性グアニル酸シクラーゼ / ヌクレオチド / 低分子シグナル分子 / ヘム鉄 / アジド / 5配位高スピン型 / YC-1 / 一酸化窒素(NO) / EXAFS / alky1 isocyanide / 酸素化型ヘム / ガス状シグナル分子 |
|---|
| Research Abstract |
We have revealed that there were two kinds of nucleotide binding sites, a catalytic and a pseudo-nucleotide sites in soluble guanylate cyclase. When carbon monoxide combined to the enzymic heme, the binding of YC-1 to the pseudo-nucleotide binding site increased the affinity of a nucleotide for the pseudo nucleotide binding site, through interaction between two binding sites. Furthermore, we have first confirmed the formation of the oxygenated form of the enzyme, which was stable under frozen conditions. The formation of the oxygenated form was noted to be regulated by YC-1 binding, and also was suggested to be governed by the deformation of the heme iron from the heme plane, based on the EXAFS analyses.
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