ArticlePloS one2010
Characterisation of PduS, the pdu metabolosome corrin reductase, and evidence of substructural organisation within the bacterial microcompartment.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 41 citations in OpenAlex.
- Electrochemical NAD+ regeneration in bacterial organelles.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Light-Driven Hybrid Nanoreactor Harnessing the Synergy of Carboxysomes and Organic Frameworks for Efficient Hydrogen Production.ACS catalysis · 2024Article
- 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
- Linking the Salmonella enterica 1,2-Propanediol Utilization Bacterial Microcompartment Shell to the Enzymatic Core via the Shell Protein PduB.Journal of bacteriology · 2022Article
- Biogenesis of a bacterial metabolosome for propanediol utilization.Nature communications · 2022Article
- Bacterial microcompartments for isethionate desulfonation in the taurine-degrading human-gut bacterium Bilophila wadsworthia.BMC microbiology · 2021Article
- Evolutionary relationships among shell proteins of carboxysomes and metabolosomes.Current opinion in microbiology · 2021Review
- Symmetry breaking and structural polymorphism in a bacterial microcompartment shell protein for choline utilization.Protein science : a publication of the Protein Society · 2020Article
- Decoding the stoichiometric composition and organisation of bacterial metabolosomes.Nature communications · 2020Article
- Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles.Nature communications · 2020Article
- Structural Characterization of a Synthetic Tandem-Domain Bacterial Microcompartment Shell Protein Capable of Forming Icosahedral Shell Assemblies.ACS synthetic biology · 2019Article
- Review
- Engineering nanoreactors using bacterial microcompartment architectures.Current opinion in biotechnology · 2018Review
- Bacterial microcompartments.Nature reviews. Microbiology · 2018Review
- Effect of bio-engineering on size, shape, composition and rigidity of bacterial microcompartments.Scientific reports · 2016Article
- Phylogeny and physiology of candidate phylum 'Atribacteria' (OP9/JS1) inferred from cultivation-independent genomics.The ISME journal · 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
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
PduS is a corrin reductase and is required for the reactivation of the cobalamin-dependent diol dehydratase. It is one component encoded within the large propanediol utilisation (pdu) operon, which is responsible for the catabolism of 1,2-propanediol within a self-assembled proteinaceous bacterial microcompartment. The enzyme is responsible for the reactivation of the cobalamin coenzyme required by the diol dehydratase. The gene for the cobalamin reductase from Citrobacter freundii (pduS) has been cloned to allow the protein to be overproduced recombinantly in E. coli with an N-terminal His-tag. Purified recombinant PduS is shown to be a flavoprotein with a non-covalently bound FMN that also contains two coupled [4Fe-4S] centres. It is an NADH-dependent flavin reductase that is able to mediate the one-electron reductions of cob(III)alamin to cob(II)alamin and cob(II)alamin to cob(I)alamin. The [4Fe-4S] centres are labile to oxygen and their presence affects the midpoint redox potential of flavin. Evidence is presented that PduS is able to bind cobalamin, which is inconsistent with the view that PduS is merely a flavin reductase. PduS is also shown to interact with one of the shell proteins of the metabolosome, PduT, which is also thought to contain an [Fe-S] cluster. PduS is shown to act as a corrin reductase and its interaction with a shell protein could allow for electron passage out of the bacterial microcompartment.
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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.