ArticleProceedings of the National Academy of Sciences of the United States of America2025
Structures of methane and ammonia monooxygenases in native membranes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Emerging classes of copper enzymes.Current opinion in chemical biology · 2026Review
- Membrane properties modulate methane oxidation by particulate methane monooxygenase.The Journal of biological chemistry · 2026Article
- Plant metabolic adaptation to nitrogen scarcity: the role of biological nitrification inhibitors.Essays in biochemistry · 2026Review
- HChemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Ammonia monooxygenase: a work in progress.Chemical science · 2026Review
- Unsymmetric bimetallic centres in metalloproteins and synthetic models.Nature reviews. Chemistry · 2026Review
- No evidence for the putative nitric oxide sensor NsrR as a key regulator of magnetosome formation in Magnetospirillum gryphiswaldense.Nucleic acids research · 2026Article
- Structural insights into the catalytic mechanism of ammonia monooxygenase.Nature communications · 2025Article
- Advances in native cell membrane nanoparticles system.Current opinion in structural biology · 2025Review
- A Molecular Mechanism for the Reduction of the Cu Site in Lytic Polysaccharide Monooxygenases by Phenol Reductants.JACS Au · 2025Article
- Recent Advances in Bioinspired Cu-Directed C-H Hydroxylation Reactions.Accounts of chemical research · 2025Article
- Harnessing the potential of microbial methane utilization for chasing sustainability.Current opinion in biotechnology · 2025Review
- Research on nitrogen transformation pathways of a thermophilic heterotrophic nitrifying bacterial consortium GW7.Frontiers in microbiology · 2025Article
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Authors and funding
2 authors.
Funding
Abstract
Methane- and ammonia-oxidizing bacteria play key roles in the global carbon and nitrogen cycles, respectively. These bacteria use homologous copper membrane monooxygenases to accomplish the defining chemical transformations of their metabolisms: the oxidations of methane to methanol by particulate methane monooxygenase (pMMO) and ammonia to hydroxylamine by ammonia monooxygenase (AMO), enzymes of prime interest for applications in mitigating climate change. However, investigations of these enzymes have been hindered by the need for disruptive detergent solubilization prior to structure determination, confounding studies of pMMO and precluding studies of AMO. Here, we overcome these challenges by using cryoEM to visualize pMMO and AMO directly in their native membrane arrays at 2.4 to 2.8 Å resolution. These structures reveal details of the copper centers, numerous bound lipids, and previously unobserved components, including identifiable and distinct supernumerary helices interacting with pMMO and AMO, suggesting a widespread role for these helices in copper membrane monooxygenases. Comparisons between these structures, their metallocofactors, and their unexpected protein-protein interactions highlight features that may govern activity or the formation of higher-order arrays in native membranes. The ability to obtain molecular insights within the native membrane will enable further understanding of these environmentally important enzymes.
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