Particulate methane monooxygenase contains only mononuclear copper centers

Ross, Matthew O, MacMillan, Fraser ORCID: https://orcid.org/0000-0002-2410-4790, Wang, Jingzhou, Nisthal, Alex, Lawton, Thomas J, Olafson, Barry D, Mayo, Stephen L, Rosenzweig, Amy C and Hoffman, Brian M (2019) Particulate methane monooxygenase contains only mononuclear copper centers. Science, 364 (6440). pp. 566-570. ISSN 0036-8075

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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.

Item Type:	Article
Additional Information:	Copyright © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.
Faculty \ School:	Faculty of Science > School of Chemistry (former - to 2024)
UEA Research Groups:	Faculty of Science > Research Groups > Chemistry of Life Processes Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Chemistry of Light and Energy
Depositing User:	LivePure Connector
Date Deposited:	09 Jul 2019 13:22
Last Modified:	18 Oct 2024 23:50
URI:	https://ueaeprints.uea.ac.uk/id/eprint/71687
DOI:	10.1126/science.aav2572

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