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Particulate methane monooxygenase contains only mononuclear copper centers

Ross, Matthew O. and MacMillan, Fraser and Wang, Jingzhou and Nisthal, Alex and Lawton, Thomas J. and Olafson, Barry D. and Mayo, Stephen L. and 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. PMCID PMC6664434. doi:10.1126/science.aav2572.

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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_B) and one ~2 nanometers away in the membrane-bound PmoC subunit (Cu_C). 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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URLURL TypeDescription Materials CentralArticle
Mayo, Stephen L.0000-0002-9785-5018
Hoffman, Brian M.0000-0002-3100-0746
Additional Information:© 2019 American Association for the Advancement of Science. This is an article distributed under the terms of the Science Journals Default License. Received 29 August 2018; accepted 15 April 2019. We thank G. E. Cutsail III, M. A. Culpepper, and H. W. Pinkett for helpful discussions as well as an anonymous reviewer for the expert analysis of the Gaussian fitting and providing above and beyond effort. This work was supported by NIH grants GM118035 (A.C.R.), GM111097 (B.M.H.), and 5T32GM008382 (M.O.R.) and NSF grant 1534743 (S.L.M., B.D.O., and A.C.R.). F.M. was supported by a Royal Society Wolfson Research Merit Award. Author contributions: M.O.R, F.M., A.N., T.J.L., B.D.O, S.L.M., A.C.R., and B.M.H. designed experiments. M.O.R., F.M., J.W., and A.N. carried out experiments. M.O.R, A.C.R., and B.M.H. wrote the manuscript. Competing interests: A patent related to this work has been issued: A. C. Rosenzweig, T. J. Lawton, A. Nisthal, J. S. Kostecki, H. K. Privett, F. Lee, B. Olafson, A. D. Dousis, “Engineered recombinant enzymes for methane oxidation” U.S. patent US9896700B2. B.D.O. is a cofounder and the CEO of Protabit, a for-profit company that develops and markets software for protein engineering and computational protein design. S.L.M. is a cofounder of Protabit. Data and materials availability: All data are available in the manuscript or the supplementary materials.
Funding AgencyGrant Number
NIH Predoctoral Fellowship5T32GM008382
Issue or Number:6440
PubMed Central ID:PMC6664434
Record Number:CaltechAUTHORS:20190509-152916236
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Official Citation:Particulate methane monooxygenase contains only mononuclear copper centers. BY MATTHEW O. ROSS, FRASER MACMILLAN, JINGZHOU WANG, ALEX NISTHAL, THOMAS J. LAWTON, BARRY D. OLAFSON, STEPHEN L. MAYO, AMY C. ROSENZWEIG, BRIAN M. HOFFMAN. SCIENCE 10 MAY 2019 : 566-570; doi: 10.1126/science.aav2572
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:95384
Deposited By: Tony Diaz
Deposited On:09 May 2019 22:50
Last Modified:16 Nov 2021 17:12

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