ArticleJournal of bacteriology2014
Enzymatic characterization and in vivo function of five terminal oxidases in Pseudomonas aeruginosa.
Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.
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74 citing papers in PubMed, 127 citations in OpenAlex.
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- Oxygen scavenging enables microoxic survival of the marine anammox bacterium Scalindua sp.The ISME journal · 2026Article
- Essential role of cytochromeFrontiers in cellular and infection microbiology · 2026Article
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- Sulphide and oleic acid synergism in accelerating mcl-PHA biopolymer production inBiochemistry and biophysics reports · 2025Article
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- Insights into the diverse roles of the terminal oxidases in Burkholderia cenocepacia H111.Scientific reports · 2025Article
- Identification of determinants that allow maintenance of high-level fluoroquinolone resistance inmBio · 2025Article
- Comparative genome analysis reveals broad phylogenetic and functional diversity within the order Nitrospirales.The ISME journal · 2025Article
- PA5402-5407 of Pseudomonas aeruginosa Regulate the Expression of the Aa3-Type Oxidases and Their Growth Under Carbon Starvation and High-Density Conditions.Current microbiology · 2024Article
- Identification of Determinants that Allow Maintenance of High-Level Fluoroquinolone Resistance inbioRxiv : the preprint server for biology · 2024Article
- Improvement of a mouse infection model to captureProceedings of the National Academy of Sciences of the United States of America · 2024Article
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- The structure of the diheme cytochrome cJournal of inorganic biochemistry · 2024Article
- Cyanide Insensitive Oxidase Confers Hydrogen Sulfide and Nitric Oxide Tolerance toAntioxidants (Basel, Switzerland) · 2024Article
14 more citing papers are in PubMed but not listed here.
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6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ubiquitous opportunistic pathogen Pseudomonas aeruginosa has five aerobic terminal oxidases: bo(3)-type quinol oxidase (Cyo), cyanide-insensitive oxidase (CIO), aa3-type cytochrome c oxidase (aa3), and two cbb(3)-type cytochrome c oxidases (cbb(3)-1and cbb(3)-2). These terminal oxidases are differentially regulated under various growth conditions and are thought to contribute to the survival of this microorganism in a wide variety of environmental niches. Here, we constructed multiple mutant strains of P. aeruginosa that express only one aerobic terminal oxidase to investigate the enzymatic characteristics and in vivo function of each enzyme. The Km values of Cyo, CIO, and aa3 for oxygen were similar and were 1 order of magnitude higher than those of cbb(3)-1 and cbb(3)-2, indicating that Cyo, CIO, and aa3 are low-affinity enzymes and that cbb(3)-1 and cbb(3)-2 are high-affinity enzymes. Although cbb(3)-1 and cbb(3)-2 exhibited different expression patterns in response to oxygen concentration, they had similar Km values for oxygen. Both cbb(3)-1 and cbb(3)-2 utilized cytochrome c4 as the main electron donor under normal growth conditions. The electron transport chains terminated by cbb(3)-1 and cbb(3)-2 generate a proton gradient across the cell membrane with similar efficiencies. The electron transport chain of aa3 had the highest proton translocation efficiency, whereas that of CIO had the lowest efficiency. The enzymatic properties of the terminal oxidases reported here are partially in agreement with their regulatory patterns and may explain the environmental adaptability and versatility of P. aeruginosa.
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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.