ArticleBiochemistry2014
Structure and protein-protein interactions of methanol dehydrogenase from Methylococcus capsulatus (Bath).
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- A systems-level view of metabolic impact of copper and methane valorization potential inMetabolic engineering communications · 2026Article
- Harnessing the potential of microbial methane utilization for chasing sustainability.Current opinion in biotechnology · 2025Review
- Structure-driven development of a biomimetic rare earth artificial metalloprotein.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Physiological basis for atmospheric methane oxidation and methanotrophic growth on air.Nature communications · 2024Article
- Direct Methane Oxidation by Copper- and Iron-Dependent Methane Monooxygenases.Chemical reviews · 2024Review
- Structure and activity of particulate methane monooxygenase arrays in methanotrophs.Nature communications · 2022Article
- Metal(loid) speciation and transformation by aerobic methanotrophs.Microbiome · 2021Review
- Bioinorganic insights of the PQQ-dependent alcohol dehydrogenases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021Review
- Biochemistry of aerobic biological methane oxidation.Chemical Society reviews · 2021Review
- Switching Between Methanol Accumulation and Cell Growth by Expression Control of Methanol Dehydrogenase inFrontiers in microbiology · 2021Article
- Biological pincer complexes.ChemCatChem · 2020Article
- Lanthanide-dependent alcohol dehydrogenases require an essential aspartate residue for metal coordination and enzymatic function.The Journal of biological chemistry · 2020Article
- Widespread soil bacterium that oxidizes atmospheric methane.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Efficient Counterselection for Methylococcus capsulatus (Bath) by Using a MutatedApplied and environmental microbiology · 2018Article
- Structure and function of the lanthanide-dependent methanol dehydrogenase XoxF from the methanotroph Methylomicrobium buryatense 5GB1C.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- The crystal structure of methanol dehydrogenase, a quinoprotein from the marine methylotrophic bacterium Methylophaga aminisulfidivorans MPJournal of microbiology (Seoul, Korea) · 2018Article
- A Genome-Scale Metabolic Model forFrontiers in microbiology · 2018Article
- Rare Earth Elements Alter Redox Balance inFrontiers in microbiology · 2018Article
- A tale of two methane monooxygenases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Review
- Biocatalysts for methane conversion: big progress on breaking a small substrate.Current opinion in chemical biology · 2016Review
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2 authors.
Funding
Abstract
In the initial steps of their metabolic pathway, methanotrophic bacteria oxidize methane to methanol with methane monooxygenases (MMOs) and methanol to formaldehyde with methanol dehydrogenases (MDHs). Several lines of evidence suggest that the membrane-bound or particulate MMO (pMMO) and MDH interact to form a metabolic supercomplex. To further investigate the possible existence of such a supercomplex, native MDH from Methylococcus capsulatus (Bath) has been purified and characterized by size exclusion chromatography with multi-angle light scattering and X-ray crystallography. M. capsulatus (Bath) MDH is primarily a dimer in solution, although an oligomeric species with a molecular mass of ∼450-560 kDa forms at higher protein concentrations. The 2.57 Å resolution crystal structure reveals an overall fold and α2β2 dimeric architecture similar to those of other MDH structures. In addition, biolayer interferometry studies demonstrate specific protein-protein interactions between MDH and M. capsulatus (Bath) pMMO as well as between MDH and the truncated recombinant periplasmic domains of M. capsulatus (Bath) pMMO (spmoB). These interactions exhibit KD values of 833 ± 409 nM and 9.0 ± 7.7 μM, respectively. The biochemical data combined with analysis of the crystal lattice interactions observed in the MDH structure suggest a model in which MDH and pMMO associate not as a discrete, stoichiometric complex but as a larger assembly scaffolded by the intracytoplasmic membranes.
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