The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Methane-Oxidizing Enzymes: An Upstream Problem in Biological Gas-to-Liquids Conversion
Open accessAbstract
Biological conversion of natural gas to liquids (Bio-GTL) represents an immense economic opportunity. In nature, aerobic methanotrophic bacteria and anaerobic archaea are able to selectively oxidize methane using methane monooxygenase (MMO) and methyl coenzyme M reductase (MCR) enzymes. Although significant progress has been made toward genetically manipulating these organisms for biotechnological applications, the enzymes themselves are slow, complex, and not recombinantly tractable in traditional industrial hosts. With turnover numbers of 0.16-13 s(-1), these enzymes pose a considerable upstream problem in the biological production of fuels or chemicals from methane. Methane oxidation enzymes will need to be engineered to be faster to enable high volumetric productivities; however, efforts to do so and to engineer simpler enzymes have been minimally successful. Moreover, known methane-oxidizing enzymes have different expression levels, carbon and energy efficiencies, require auxiliary systems for biosynthesis and function, and vary considerably in terms of complexity and reductant requirements. The pros and cons of using each methane-oxidizing enzyme for Bio-GTL are considered in detail. The future for these enzymes is bright, but a renewed focus on studying them will be critical to the successful development of biological processes that utilize methane as a feedstock.
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Cites
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The Moderately Efficient Enzyme: Evolutionary and Physicochemical Trends Shaping Enzyme Parameters
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How to Make a Living by Exhaling Methane
Ferry, J. G. (2010) · Annual Review of Microbiology · doi:10.1146/annurev.micro.112408.134051 · Cited by 177
Cited by
Bioinspired Metal–Organic Framework Catalysts for Selective Methane Oxidation to Methanol
Baek, J., Rungtaweevoranit, B., Pei, X., Park, M., Fakra, S. C., Liu, Y.-S., Matheu, R., Alshmimri, S. A., Alshehri, S., Trickett, C. A., et al. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b11525 · Cited by 417
Making quantitative sense of electromicrobial production
Claassens, N. J., Cotton, C. A. R., Kopljar, D., & Bar-Even, A. (2019) · Nature Catalysis · doi:10.1038/s41929-019-0272-0 · Cited by 303
Particulate methane monooxygenase contains only mononuclear copper centers
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) · Science · doi:10.1126/science.aav2572 · Cited by 293
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Metadata
- Authors
- Lawton, T. J., & Rosenzweig, A. C.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2016-07-19
- Volume
- 138
- Issue
- 30
- Pages
- 9327-9340
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2462210636
- Cited by
- 164
- References
- 5
- FWCI
- 8.73
- Type
- journal article
- Language
- en
- Open access
- green
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