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 |
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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 |
Depositing User: | LivePure Connector |
Date Deposited: | 09 Jul 2019 13:22 |
Last Modified: | 15 Aug 2022 03:10 |
URI: | https://ueaeprints.uea.ac.uk/id/eprint/71687 |
DOI: | 10.1126/science.aav2572 |
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