Construction and regulation of the reactivity of metalloenzyme models containing hydrophobic micro-space
| Project/Area Number |
26410072
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Inorganic chemistry
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| Research Institution | Osaka University |
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Principal Investigator |
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2016: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2015: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2014: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | 生物無機化学 / 酵素 / モデル / 疎水空間 / 水素結合 / 鉄－硫黄クラスター / モリブデン / マグネシウム / ニトロゲナーゼ |
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| Outline of Final Research Achievements |
Model complexes of metalloproteins containing “hydrophobic micro-space” were synthesized and their properties were investigated. Molybdenum- and tungsten-enzyme models showed enhancement of the oxygen-atom-transfer reaction of trimethylamine N-oxide or dimethyl sulfoxide by efficient uptake of the substrate into the active site in hydrophobic environment．Modeling of the hydrophobic microenvironment of water-soluble molybdenum enzyme in an aqueous micellar solution was successfully achieved. Unexpected reaction promoted by hydrogen bond in nonpolar solvents was observed. The regulation the hydrolytic activity of magnesium-containing phosphatase models by switching the mode of NH…O hydrogen bond was accomplished in nonpolar solvents. The combination of the hydrophobic space and NH…S hydrogen bonds also regulated the electronic structure of [4Fe4S] cluster in a ferredoxin model.
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Report
(4 results)
Research Products
(24 results)
