The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
Particulate methane monooxygenase contains only mononuclear copper centers
Open accessAbstract
How many metals to oxidize methane?: Methane is an important fuel, but there are few direct transformations to partially oxidized products. Bacteria use metalloenzymes to catalyze methane oxidation to methanol, a reaction of industrial interest. Understanding the metal sites that enable this reaction may inspire new biomimetic catalysts. Ross et al. used spectroscopic measurements to assign two monocopper sites in the enzyme particulate methane monooxygenase. These results differ in part from previous proposals for the location and nuclearity of the metal sites and will prompt rethinking about how this metalloenzyme catalyzes methane oxidation. Science , this issue p. 566
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Cites
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Self-citationMethane Activation by Heterogeneous Catalysis
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Oxidation of methane by a biological dicopper centre
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Self-citationEnvironmental, genomic and taxonomic perspectives on methanotrophic Verrucomicrobia
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Alkane Oxidation: Methane Monooxygenases, Related Enzymes, and Their Biomimetics
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Zhang, Q., Yu, J., & Corma, A. (2020) · Advanced Materials · doi:10.1002/adma.202002927 · Cited by 316
Unexpected complexity of the ammonia monooxygenase in archaea
(2023) · doi:10.1038/s41396-023-01367-3 · Cited by 58
Metadata
- Authors
- Ross, M. O., MacMillan, F., Wang, J., Nisthal, A., Lawton, T. J., Olafson, B. D., Mayo, S. L., Rosenzweig, A. C., & Hoffman, B. M.
- Venue
- Science
- Published
- 2019-05-10
- Volume
- 364
- Issue
- 6440
- Pages
- 566-570
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2944342539
- Cited by
- 293
- References
- 40
- FWCI
- 15.58
- Type
- journal article
- Language
- en
- Open access
- green
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- Ross, M. O., MacMillan, F., Wang, J., Nisthal, A., Lawton, T. J., Olafson, B. D., Mayo, S. L., Rosenzweig, A. C., & Hoffman, B. M. (2019). Particulate methane monooxygenase contains only mononuclear copper centers. Science. https://doi.org/10.1126/science.aav2572
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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