2012 Fiscal Year Final Research Report
Activity of copper enzymes and new development of quantum calculation
| Project/Area Number |
21750063
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Inorganic chemistry
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| Research Institution | Kyushu University |
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Principal Investigator |
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| Project Period (FY) |
2009 – 2012
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| Keywords | 基礎化学 / 無機化学 |
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| Research Abstract |
Methane hydroxylation at the dinuclear copper site of particulate methane monooxygenase (pMMO) is studied by using density functional theory calculations. The electronic, structural, and reactive properties of a possible dinuclear copper species (n-oxo)(n-hydroxo)CuIICuIIIare discussed with respect to the C-H bond activation of methane.We propose that the Tyr374 residue in the second coordination sphere of the dicopper site donates an H atom to the n-n2:n2-peroxoCuIICuIIspecies and the resultant (n-oxo)(n-hydroxo)CuIICuIIIspecies is able to hydroxylate methane. This species for methane hydroxylation is more favorable in reactivity than the bis(n-oxo)CuIIICuIIIspecies. The H-atom transfer or proton-coupled electron transfer from the tyrosine residue can reasonably induce the O-O bond dissociation of the n-n2:n2-peroxoCuIICuIIspecies to form the reactive (n-oxo)(n-hydroxo)CuIICuIIIspecies, which is expected to be an active species for the conversion of methane to methanol at the dicopper site of pMMO
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