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  • Title: Role of tyrosine residue in methane activation at the dicopper site of particulate methane monooxygenase: a density functional theory study.
    Author: Shiota Y, Juhász G, Yoshizawa K.
    Journal: Inorg Chem; 2013 Jul 15; 52(14):7907-17. PubMed ID: 23808646.
    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 reactivity properties of a possible dinuclear copper species (μ-oxo)(μ-hydroxo)Cu(II)Cu(III) are discussed with respect to the C-H bond activation of methane. We propose that the tyrosine residue in the second coordination sphere of the dicopper site donates an H atom to the μ-η(2):η(2)-peroxoCu(II)Cu(II) species and the resultant (μ-oxo)(μ-hydroxo)Cu(II)Cu(III) species can hydroxylate methane. This species for methane hydroxylation is more favorable in reactivity than the bis(μ-oxo)Cu(III)Cu(III) species. The H-atom transfer or proton-coupled electron transfer from the tyrosine residue can reasonably induce the O-O bond dissociation of the μ-η(2):η(2)-peroxoCu(II)Cu(II) species to form the reactive (μ-oxo)(μ-hydroxo)Cu(II)Cu(III) species, which is expected to be an active species for the conversion of methane to methanol at the dicopper site of pMMO. The rate-determining step for the methane hydroxylation is the C-H cleavage, which is in good agreement with experimental KIE values reported so far.
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