Construction of Engineered Myoglobin toward a Catalyst for Alkane Hydroxylation
| Project/Area Number |
26620045
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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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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| Co-Investigator(Renkei-kenkyūsha) |
OOHORA Koji 大阪大学, 大学院工学研究科, 助教 (10631202)
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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 |
¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2015: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2014: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | ミオグロビン / 再構成 / マンガンポルフィセン / 水酸化 / 水酸化反応 / 人工生体金属触媒 / 人工生体触媒 |
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| Outline of Final Research Achievements |
Myoglobin, an O2-storage hemoprotein, shows very low peroxidase and monooxygenase activities and does not catalyze alkane hydroxylation, although myoglobin possesses the same cofactor, heme b, as seen in a series of heme-dependent enzymes such as horseradish peroxidase and cytochrome P450. Our group previously reported that myoglobin reconstituted with manganese porphycene catalyzes C-H bond hydroxylation using H2O2 as a terminal oxidant. In this study, we have demonstrated that reconstituted myoglobin mutants accelerate the hydroxylation of the inert alkane substrates with high enantioselectivity and catalytic activity. The active intermediate was assigned as the Mn(V)-oxo species by spectroscopic measurements. Based on these findings, several mutants were further designed. The mutants are found to improve the enantioselectivity for chiral alcohol products and show catalytic activity for hydroxylation of more inert alkanes such as hexane.
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Report
(4 results)
Research Products
(12 results)
