ArticleThe Journal of biological chemistry2016
Metabolite-driven Regulation of Heme Uptake by the Biliverdin IXβ/δ-Selective Heme Oxygenase (HemO) of Pseudomonas aeruginosa.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 38 citations in OpenAlex.
- Porphyrin pathways as targets for combating antimicrobial resistance: virulence and therapeutic opportunities.Frontiers in cellular and infection microbiology · 2026Review
- Heme in Bacterial Pathogenesis and as an Antimicrobial Target.Chemical reviews · 2025Review
- The Pseudomonas aeruginosa PhuS proximal ligand His-209 triggers a conformational switch in function from DNA binding to heme transfer.The Journal of biological chemistry · 2025Article
- Article
- Iron-responsive riboswitches.Current opinion in chemical biology · 2022Review
- Modeling the native ensemble of PhuS using enhanced sampling MD and HDX-ensemble reweighting.Biophysical journal · 2021Article
- Review
- Axial Heme Coordination by the Tyr-His Motif in the Extracellular Hemophore HasAp Is Critical for the Release of Heme to the HasR Receptor ofBiochemistry · 2021Article
- Extracellular haem utilization by the opportunistic pathogen Pseudomonas aeruginosa and its role in virulence and pathogenesis.Advances in microbial physiology · 2021Article
- Recombinant Production of Biliverdin IXβ and δ Isomers in the T7 Promoter CompatibleFrontiers in microbiology · 2021Article
- Metallotherapeutics development in the age of iron-clad bacteria.Metallomics : integrated biometal science · 2020Review
- Gallium(III)-Salophen as a Dual Inhibitor ofACS infectious diseases · 2020Article
- Contributions of the heme coordinating ligands of theThe Journal of biological chemistry · 2020Article
- Heme uptake and utilization by hypervirulent Acinetobacter baumannii LAC-4 is dependent on a canonical heme oxygenase (abHemO).Archives of biochemistry and biophysics · 2019Article
- Post-transcriptional regulation of theThe Journal of biological chemistry · 2019Article
- Heme Uptake and Utilization by Gram-Negative Bacterial Pathogens.Frontiers in cellular and infection microbiology · 2019Review
- The affinity of MhuD for heme is consistent with a heme degrading function in vivo.Metallomics : integrated biometal science · 2018Article
- The Asp99-Arg188 salt bridge of the Pseudomonas aeruginosa HemO is critical in allowing conformational flexibility during catalysis.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Heme degradation enzyme biliverdin IXβ reductase is required for stem cell glutamine metabolism.The Biochemical journal · 2018Article
- PAMDB: a comprehensive Pseudomonas aeruginosa metabolome database.Nucleic acids research · 2018Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Pseudomonas aeruginosa acquires extracellular heme via the Phu (Pseudomonas heme uptake) and Has (heme assimilation system) systems. We have previously shown the catalytic actions of heme oxygenase (HemO) along with the cytoplasmic heme transport protein PhuS control heme flux into the cell. To further investigate the role of the PhuS-HemO couple in modulating heme uptake, we have characterized two HemO variants, one that is catalytically inactive (HemO H26A/K34A/K132A or HemOin) and one that has altered regioselectivity (HemO N19K/K34A/F117Y/K132A or HemOα), producing biliverdin IXα (BVIXα). HemOα similar to wild type was able to interact and acquire heme from holo-PhuS. In contrast, the HemOin variant did not interact with holo-PhuS and showed no enzymatic activity. Complementation of a hemO deletion strain with the hemOin or hemOα variants in combination with [(13)C]heme isotopic labeling experiments revealed that the absence of BVIXβ and BVIXδ leads to a decrease in extracellular levels of hemophore HasA. We propose BVIXβ and/or BVIXδ transcriptionally or post-transcriptionally regulates HasA. Thus, coupling the PhuS-dependent flux of heme through HemO to feedback regulation of the cell surface signaling system through HasA allows P. aeruginosa to rapidly respond to fluctuating extracellular heme levels independent of the iron status of the cell.
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Registered trials
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