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Particulate methane monooxygenase contains only mononuclear copper centers.


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 (CuB) and one ~2 nanometers away in the membrane-bound PmoC subunit (CuC). On the basis of these results, we propose that a monocopper site is able to catalyze methane oxidation in pMMO.

SUBMITTER: Ross MO 

PROVIDER: S-EPMC6664434 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature

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Particulate methane monooxygenase contains only mononuclear copper centers.

Ross Matthew O MO   MacMillan Fraser F   Wang Jingzhou J   Nisthal Alex A   Lawton Thomas J TJ   Olafson Barry D BD   Mayo Stephen L SL   Rosenzweig Amy C AC   Hoffman Brian M BM  

Science (New York, N.Y.) 20190501 6440


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 pM  ...[more]

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2019-04-24 | MSV000083717 | MassIVE