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Particulate methane monooxygenase contains only mononuclear copper centers. | LitMetric

AI Article Synopsis

  • * Researchers explored the controversial structure of the copper active site in the enzyme called particulate methane monooxygenase (pMMO) using biochemical and spectroscopic techniques.
  • * The findings suggest that pMMO contains two monocopper sites, one in the soluble PmoB subunit and another in the membrane-bound PmoC subunit, which together may facilitate the oxidation of methane.

Article Abstract

Bacteria that oxidize methane to methanol are central to mitigating emissions of methane, a potent greenhouse gas. The nature of the copper active site in the primary metabolic enzyme of these bacteria, particulate methane monooxygenase (pMMO), has been controversial owing to seemingly contradictory biochemical, spectroscopic, and crystallographic results. We present biochemical and electron paramagnetic resonance spectroscopic characterization most consistent with two monocopper sites within pMMO: one in the soluble PmoB subunit at the previously assigned active site (Cu) and one ~2 nanometers away in the membrane-bound PmoC subunit (Cu). On the basis of these results, we propose that a monocopper site is able to catalyze methane oxidation in pMMO.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6664434PMC
http://dx.doi.org/10.1126/science.aav2572DOI Listing

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