ReviewJournal of the American Chemical Society2016
Methane-Oxidizing Enzymes: An Upstream Problem in Biological Gas-to-Liquids Conversion.
Review in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
41 citing papers in PubMed, 164 citations in OpenAlex.
- Article
- Assessment and functional genomic investigation of methane and nitrogen metabolizing pathways in Pseudomonas aeruginosa strain AAK/M5.World journal of microbiology & biotechnology · 2026Article
- Industrial applicability of enzymatic and whole-cell processes for the utilization of C1 building blocks.Nature communications · 2025Review
- Advancements in the production of value-added products via methane biotransformation by methanotrophs: Current status and future perspectives.Journal of microbiology (Seoul, Korea) · 2025Review
- Production of Novel Energy Gases in Bioprocesses Using Undefined Mixed Cultures.Advances in biochemical engineering/biotechnology · 2025Review
- Evaluation of microbial community dynamics and chlorinated solvent biodegradation in methane-amended microcosms from an acidic aquifer.Biodegradation · 2024Article
- Expanding the Clip-and-Cleave Concept: Approaching Enantioselective C-H Hydroxylations by Copper Imine Complexes Using OJournal of the American Chemical Society · 2024Article
- Toward the Use of Methyl-Coenzyme M Reductase for Methane Bioconversion Applications.Accounts of chemical research · 2024Article
- Capturing methane with recombinant soluble methane monooxygenase and recombinant methyl-coenzyme M reductase.Microbial biotechnology · 2024Review
- Direct Methane Oxidation by Copper- and Iron-Dependent Methane Monooxygenases.Chemical reviews · 2024Review
- Product analog binding identifies the copper active site of particulate methane monooxygenase.Nature catalysis · 2023Article
- Recombinant expression and subcellular targeting of the particulate methane monooxygenase (pMMO) protein components in plants.Scientific reports · 2023Article
- Acidophilic methanotrophs: Occurrence, diversity, and possible bioremediation applications.Environmental microbiology reports · 2023Review
- Transcriptional and metabolomic responses ofFrontiers in microbiology · 2023Article
- Recent Insights into Cu-Based Catalytic Sites for the Direct Conversion of Methane to Methanol.Molecules (Basel, Switzerland) · 2022Review
- Microorganisms harbor keys to a circular bioeconomy making them useful tools in fighting plastic pollution and rising COExtremophiles : life under extreme conditions · 2022Article
- Overview of Diverse Methyl/Alkyl-Coenzyme M Reductases and Considerations for Their Potential Heterologous Expression.Frontiers in microbiology · 2022Review
- Recent trends of biotechnological production of polyhydroxyalkanoates from C1 carbon sources.Frontiers in bioengineering and biotechnology · 2022Review
- Atmospheric methane removal: a research agenda.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2021Article
- Coordination of the Copper Centers in Particulate Methane Monooxygenase: Comparison between Methanotrophs and Characterization of the CuJournal of the American Chemical Society · 2021Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
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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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.