ArticleNature communications2019
Native top-down mass spectrometry provides insights into the copper centers of membrane-bound methane monooxygenase.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 99 citations in OpenAlex.
- Article
- Membrane properties modulate methane oxidation by particulate methane monooxygenase.The Journal of biological chemistry · 2026Article
- Determination of Thermochemical Barriers in Multiple-Collision-Induced Dissociation Experiments on Gas-Phase Protein Complexes.Journal of the American Chemical Society · 2025Article
- Critical evaluation of three cryo-EM structures of particulate methane monooxygenase by quantum refinement.Acta crystallographica. Section D, Structural biology · 2025Article
- Uncovering hidden protein modifications with native top-down mass spectrometry.Nature methods · 2025Article
- Structural Heterogeneity of Proteoform-Ligand Complexes in Adenosine Monophosphate-Activated Protein Kinase Uncovered by Integrated Top-Down Mass Spectrometry.Journal of the American Chemical Society · 2025Article
- Imaging and spatially resolved mass spectrometry applications in nephrology.Nature reviews. Nephrology · 2025Review
- Direct Methane to Methanol Conversion: An Overview of Non-Syn Gas Catalytic Strategies.Chemical record (New York, N.Y.) · 2025Review
- Structures of methane and ammonia monooxygenases in native membranes.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Top-down mass spectrometry of native proteoforms and their complexes: a community study.Nature methods · 2024Article
- Online Mixed-Bed Ion Exchange Chromatography for Native Top-Down Proteomics of Complex Mixtures.Journal of proteome research · 2024Article
- An intramolecular macrocyclase in plant ribosomal peptide biosynthesis.Nature chemical biology · 2024Article
- Probing the functional hotspots inside protein hydrophobic pockets byChemical science · 2024Article
- 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
- Immunocomplexed Antigen Capture and Identification by Native Top-Down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2023Article
- Infrared Photoactivation Enables Improved Native Top-Down Mass Spectrometry of Transmembrane Proteins.Analytical chemistry · 2023Article
- Infrared Multiphoton Dissociation Enables Top-Down Characterization of Membrane Protein Complexes and G Protein-Coupled Receptors.Angewandte Chemie (International ed. in English) · 2023Article
- Infrared Multiphoton Dissociation Enables Top-Down Characterization of Membrane Protein Complexes and G Protein-Coupled Receptors.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023Article
- Capillary Zone Electrophoresis-Tandem Mass Spectrometry for Top-Down Proteomics of Mouse Brain Integral Membrane Proteins.Analytical chemistry · 2023Article
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Authors and funding
11 authors at 1 institution in 1 country.
Funding
Abstract
Aerobic methane oxidation is catalyzed by particulate methane monooxygenase (pMMO), a copper-dependent, membrane metalloenzyme composed of subunits PmoA, PmoB, and PmoC. Characterization of the copper active site has been limited by challenges in spectroscopic analysis stemming from the presence of multiple copper binding sites, effects of detergent solubilization on activity and crystal structures, and the lack of a heterologous expression system. Here we utilize nanodiscs coupled with native top-down mass spectrometry (nTDMS) to determine the copper stoichiometry in each pMMO subunit and to detect post-translational modifications (PTMs). These results indicate the presence of a mononuclear copper center in both PmoB and PmoC. pMMO-nanodisc complexes with a higher stoichiometry of copper-bound PmoC exhibit increased activity, suggesting that the PmoC copper site plays a role in methane oxidation activity. These results provide key insights into the pMMO copper centers and demonstrate the ability of nTDMS to characterize complex membrane-bound metalloenzymes.
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