Particulate methane monooxygenase contains only mononuclear copper centers

Matthew O. Ross, Fraser MacMillan, Jingzhou Wang, Alex Nisthal, Thomas J. Lawton, Barry D. Olafson, Stephen L. Mayo, Amy C. Rosenzweig*, Brian M. Hoffman

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

58 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)566-570
Number of pages5
JournalScience
Volume364
Issue number6440
DOIs
StatePublished - 2019

ASJC Scopus subject areas

  • General

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