ArticleJournal of bacteriology2001
Membrane-associated quinoprotein formaldehyde dehydrogenase from Methylococcus capsulatus Bath.
Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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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.
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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.
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Who cites it
22 citing papers in PubMed, 61 citations in OpenAlex.
- Thermophilic methane oxidation is widespread in Aotearoa-New Zealand geothermal fields.Frontiers in microbiology · 2023Article
- Systems analysis of the effect of hydrogen sulfide on the growth of Methylococcus capsulatus Bath.Applied microbiology and biotechnology · 2022Article
- Ecological Aerobic Ammonia and Methane Oxidation Involved Key Metal Compounds, Fe and Cu.Life (Basel, Switzerland) · 2022Review
- Unravelling Formaldehyde Metabolism in Bacteria: Road towards Synthetic Methylotrophy.Microorganisms · 2022Review
- Metal(loid) speciation and transformation by aerobic methanotrophs.Microbiome · 2021Review
- Oxygen Generation via Water Splitting by a Novel Biogenic Metal Ion-Binding Compound.Applied and environmental microbiology · 2021Article
- Biological pincer complexes.ChemCatChem · 2020Article
- Article
- A Genome-Scale Metabolic Model forFrontiers in microbiology · 2018Article
- Methanobactin and the Link between Copper and Bacterial Methane Oxidation.Microbiology and molecular biology reviews : MMBR · 2016Review
- Transcriptomic profiling of Methylococcus capsulatus (Bath) during growth with two different methane monooxygenases.MicrobiologyOpen · 2016Article
- Isolation, sequencing, and heterologous expression of the Paecilomyces variotii gene encoding S-hydroxymethylglutathione dehydrogenase (fldA).Applied microbiology and biotechnology · 2015Article
- Structure and protein-protein interactions of methanol dehydrogenase from Methylococcus capsulatus (Bath).Biochemistry · 2014Article
- CorA is a copper repressible surface-associated copper(I)-binding protein produced in Methylomicrobium album BG8.PloS one · 2014Article
- Purification and properties of S-hydroxymethylglutathione dehydrogenase of Paecilomyces variotii no. 5, a formaldehyde-degrading fungus.AMB Express · 2012Article
- Elemental economy: microbial strategies for optimizing growth in the face of nutrient limitation.Advances in microbial physiology · 2012Review
- Trace metal requirements for microbial enzymes involved in the production and consumption of methane and nitrous oxide.Frontiers in microbiology · 2012Article
- Pirin regulates pyruvate catabolism by interacting with the pyruvate dehydrogenase E1 subunit and modulating pyruvate dehydrogenase activity.Journal of bacteriology · 2007Article
- The copper chelator methanobactin from Methylosinus trichosporium OB3b binds copper(I).Journal of the American Chemical Society · 2005Article
- Genomic insights into methanotrophy: the complete genome sequence of Methylococcus capsulatus (Bath).PLoS biology · 2004Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A membrane-associated, dye-linked formaldehyde dehydrogenase (DL-FalDH) was isolated from the obligate methylotroph Methylococcus capsulatus Bath. The enzyme was the major formaldehyde-oxidizing enzyme in cells cultured in high (above 1 micromol of Cu per mg of cell protein) copper medium and expressing the membrane-associated methane monooxygenase. Soluble NAD(P)(+)-linked formaldehyde oxidation was the major activity in cells cultured in low-copper medium and expressing the soluble methane monooxygenase (Tate and Dalton, Microbiology 145:159-167, 1999; Vorholt et al., J. Bacteriol. 180:5351-5356, 1998). The membrane-associated enzyme is a homotetramer with a subunit molecular mass of 49,500 Da. UV-visible absorption, electron paramagnetic resonance, and electrospray mass spectrometry suggest the redox cofactor of the DL-FalDH is pyrroloquinoline quinone (PQQ), with a PQQ-to-subunit stochiometry of approximately 1:1. The enzyme was specific for formaldehyde, oxidizing formaldehyde to formate, and utilized the cytochrome b(559/569) complex as the physiological electron acceptor.
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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.