ArticleJournal of bacteriology2010
Characterization of the PduS cobalamin reductase of Salmonella enterica and its role in the Pdu microcompartment.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
30 citing papers in PubMed, 49 citations in OpenAlex.
- Metagenomic Identification and Characterization of Novel Vitamin BMicroorganisms · 2025Article
- Article
- Electrochemical NAD+ regeneration in bacterial organelles.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Electrochemical cofactor recycling of bacterial microcompartments.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Electrochemical cofactor recycling of bacterial microcompartments.bioRxiv : the preprint server for biology · 2024Article
- Coordination Chemistry Controls Coenzyme BInorganic chemistry · 2023Article
- Chemical probing provides insight into the native assembly state of a bacterial microcompartment.Structure (London, England : 1993) · 2022Article
- Bacterial microcompartments for isethionate desulfonation in the taurine-degrading human-gut bacterium Bilophila wadsworthia.BMC microbiology · 2021Article
- Prokaryotic Organelles: Bacterial Microcompartments inEcoSal Plus · 2020Review
- Decoding the stoichiometric composition and organisation of bacterial metabolosomes.Nature communications · 2020Article
- Review
- Cargo encapsulation in bacterial microcompartments: Methods and analysis.Methods in enzymology · 2019Article
- The Crystal Structure of the C-Terminal Domain of the Salmonella enterica PduO Protein: An Old Fold with a New Heme-Binding Mode.Frontiers in microbiology · 2016Article
- Bioinformatic characterization of glycyl radical enzyme-associated bacterial microcompartments.Applied and environmental microbiology · 2015Article
- Bacterial microcompartments: widespread prokaryotic organelles for isolation and optimization of metabolic pathways.Molecular microbiology · 2015Review
- Exploring bacterial organelle interactomes: a model of the protein-protein interaction network in the Pdu microcompartment.PLoS computational biology · 2015Article
- A taxonomy of bacterial microcompartment loci constructed by a novel scoring method.PLoS computational biology · 2014Article
- Identification of a unique Fe-S cluster binding site in a glycyl-radical type microcompartment shell protein.Journal of molecular biology · 2014Article
- Diverse bacterial microcompartment organelles.Microbiology and molecular biology reviews : MMBR · 2014Review
- FAD binding, cobinamide binding and active site communication in the corrin reductase (CobR).Bioscience reports · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Salmonella enterica degrades 1,2-propanediol (1,2-PD) in a coenzyme B12 (adenosylcobalamin, AdoCbl)-dependent fashion. Salmonella obtains AdoCbl by assimilation of complex precursors, such as vitamin B12 and hydroxocobalamin. Assimilation of these compounds requires reduction of their central cobalt atom from Co3+ to Co2+ to Co+, followed by adenosylation to AdoCbl. In this work, the His6-tagged PduS cobalamin reductase from S. enterica was produced at high levels in Escherichia coli, purified, and characterized. The anaerobically purified enzyme reduced cob(III)alamin to cob(II)alamin at a rate of 42.3±3.2 μmol min(-1) mg(-1), and it reduced cob(II)alamin to cob(I)alamin at a rate of 54.5±4.2 nmol min(-1) mg(-1) protein. The apparent Km values of PduS-His6 were 10.1±0.7 μM for NADH and 67.5±8.2 μM for hydroxocobalamin in cob(III)alamin reduction. The apparent Km values for cob(II)alamin reduction were 27.5±2.4 μM with NADH as the substrate and 72.4±9.5 μM with cob(II)alamin as the substrate. High-performance liquid chromatography (HPLC) and mass spectrometry (MS) indicated that each monomer of PduS contained one molecule of noncovalently bound flavin mononucleotide (FMN). Genetic studies showed that a pduS deletion decreased the growth rate of Salmonella on 1,2-PD, supporting a role in cobalamin reduction in vivo. Further studies demonstrated that the PduS protein is a component of the Pdu microcompartments (MCPs) used for 1,2-PD degradation and that it interacts with the PduO adenosyltransferase, which catalyzes the terminal step of AdoCbl synthesis. These studies further characterize PduS, an unusual MCP-associated cobalamin reductase, and, in conjunction with prior results, indicate that the Pdu MCP encapsulates a complete cobalamin assimilation system.
Indexed as
Identifiers
What OpenQuestion holds
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.