Role of tyrosine residue in methane activation at the dicopper site of particulate methane monooxygenase: A density functional theory study

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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)CuIICuIII 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-η22-peroxoCu IICuII species and the resultant (μ-oxo)(μ-hydroxo) CuIICuIII species can hydroxylate methane. This species for methane hydroxylation is more favorable in reactivity than the bis(μ-oxo)CuIIICuIII 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-η22- peroxoCuIICuII species to form the reactive (μ-oxo)(μ-hydroxo)CuIICuIII 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.

Original languageEnglish
Pages (from-to)7907-7917
Number of pages11
JournalInorganic chemistry
Volume52
Issue number14
DOIs
Publication statusPublished - Jul 15 2013

All Science Journal Classification (ASJC) codes

  • Physical and Theoretical Chemistry
  • Inorganic Chemistry

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