ArticleJournal of bacteriology2008
Stability of the cbb3-type cytochrome oxidase requires specific CcoQ-CcoP interactions.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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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
32 citing papers in PubMed.
- Phylogenomic and metabolic insights into iron reduction metabolism in the genusMicrobial genomics · 2026Article
- Oxygen scavenging enables microoxic survival of the marine anammox bacterium Scalindua sp.The ISME journal · 2026Article
- Article
- Functional diversity and molecular interactions of small membrane proteins in bacteria.microLife · 2025Review
- Double- or Triple-Tiered Protection: Prospects for the Sustainable Application of Copper-Based Antimicrobial Compounds for Another Fourteen Decades.International journal of molecular sciences · 2023Review
- Cryo-EM structures of engineered active bcNature communications · 2021Article
- Genes Linking Copper Trafficking and Homeostasis to the Biogenesis and Activity of theFrontiers in microbiology · 2021Article
- Cu Homeostasis in Bacteria: The Ins and Outs.Membranes · 2020Review
- TheProceedings of the National Academy of Sciences of the United States of America · 2019Article
- A Copper Relay System Involving Two Periplasmic Chaperones Drives cbbACS chemical biology · 2018Article
- Biogenesis of the bacterialThe Journal of biological chemistry · 2018Article
- Absence of Thiol-Disulfide Oxidoreductase DsbA ImpairsFrontiers in microbiology · 2017Article
- Expression of multipleProceedings of the National Academy of Sciences of the United States of America · 2016Article
- Cooperation between two periplasmic copper chaperones is required for full activity of the cbb3 -type cytochrome c oxidase and copper homeostasis in Rhodobacter capsulatus.Molecular microbiology · 2016Article
- Article
- The two transmembrane helices of CcoP are sufficient for assembly of the cbb3-type heme-copper oxygen reductase from Vibrio cholerae.Biochimica et biophysica acta · 2015Article
- Genomic characterization of Sinorhizobium meliloti AK21, a wild isolate from the Aral Sea Region.SpringerPlus · 2015Article
- The K(C) channel in the cbb3-type respiratory oxygen reductase from Rhodobacter capsulatus is required for both chemical and pumped protons.Journal of bacteriology · 2014Article
- Biochemical and biophysical characterization of the two isoforms of cbb3-type cytochrome c oxidase from Pseudomonas stutzeri.Journal of bacteriology · 2014Article
- A critical role for the cccA gene product, cytochrome c2, in diverting electrons from aerobic respiration to denitrification in Neisseria gonorrhoeae.Journal of bacteriology · 2013Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Cytochrome cbb(3)-type oxidases are members of the heme copper oxidase superfamily and are composed of four subunits. CcoN contains the heme b-Cu(B) binuclear center where oxygen is reduced, while CcoP and CcoO are membrane-bound c-type cytochromes thought to channel electrons from the donor cytochrome into the binuclear center. Like many other bacterial members of this superfamily, the cytochrome cbb(3)-type oxidase contains a fourth, non-cofactor-containing subunit, which is termed CcoQ. In the present study, we analyzed the role of CcoQ on the stability and activity of Rhodobacter capsulatus cbb(3)-type oxidase. Our data showed that CcoQ is a single-spanning membrane protein with a N(out)-C(in) topology. In the absence of CcoQ, cbb(3)-type oxidase activity is significantly reduced, irrespective of the growth conditions. Blue native polyacrylamide gel electrophoresis analyses revealed that the lack of CcoQ specifically impaired the stable recruitment of CcoP into the cbb(3)-type oxidase complex. This suggested a specific CcoQ-CcoP interaction, which was confirmed by chemical cross-linking. Collectively, our data demonstrated that in R. capsulatus CcoQ was required for optimal cbb(3)-type oxidase activity because it stabilized the interaction of CcoP with the CcoNO core complex, leading subsequently to the formation of the active 230-kDa cbb(3)-type oxidase complex.
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