ArticleMethods in enzymology2011
Metal reconstitution of particulate methane monooxygenase and heterologous expression of the pmoB subunit.
Article in Methods in enzymology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Direct Methane Oxidation by Copper- and Iron-Dependent Methane Monooxygenases.Chemical reviews · 2024Review
- A general protocol for the expression and purification of the intact transmembrane transporter FeoB.Biochimica et biophysica acta. Biomembranes · 2022Article
- Peptide hydrogel with self-healing and redox-responsive properties.Nano convergence · 2022Article
- Recovery of particulate methane monooxygenase structure and activity in a lipid bilayer.Science (New York, N.Y.) · 2022Article
- Metals and Methanotrophy.Applied and environmental microbiology · 2018Review
- Methane-Oxidizing Enzymes: An Upstream Problem in Biological Gas-to-Liquids Conversion.Journal of the American Chemical Society · 2016Review
- Structure and protein-protein interactions of methanol dehydrogenase from Methylococcus capsulatus (Bath).Biochemistry · 2014Article
- Identification of the valence and coordination environment of the particulate methane monooxygenase copper centers by advanced EPR characterization.Journal of the American Chemical Society · 2014Article
- Effects of zinc on particulate methane monooxygenase activity and structure.The Journal of biological chemistry · 2014Article
- Evidence for oxygen binding at the active site of particulate methane monooxygenase.Journal of the American Chemical Society · 2012Article
- Crystal structure and characterization of particulate methane monooxygenase from Methylocystis species strain M.Biochemistry · 2011Article
- Architecture and active site of particulate methane monooxygenase.Critical reviews in biochemistry and molecular biologyReview
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Particulate methane monooxygenase (pMMO) is a multisubunit metalloenzyme complex used by methanotrophic bacteria to oxidize methane in the first step of carbon assimilation and energy production. In this chapter, we detail methods to prepare metal free (apo) membrane-bound pMMO and to reconstitute apo pMMO with metal ions. We also describe protocols to clone, express, and refold metal-loaded soluble domain constructs of the pmoB subunit. These approaches were used to address fundamental questions concerning the metal content and location of the pMMO active site.
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Registered trials
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