Role of the tightly bound quinone for the oxygen reaction of cytochrome bo3 oxidase from Escherichia coli

Melin, Frédéric; Sabuncu, Sinan; Choi, Sung-Soon; Leprince, Agathe; Gennis, Robert B.; Hellwig, Petra

doi:10.1002/1873-3468.13263

Cited by 9 publications

(4 citation statements)

References 53 publications

(61 reference statements)

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“…Not only on eucaryon, there is now abundant literature on the three different types of CoxCs and oxidative phosphorylation that are encountered in prokaryotes (such as Rhodobacter sphaeroides, Bacillus alcalophilus, cyanobacterium Anabaena variabilis , E. coli , and Pseudomonas stutzeri ) (Cukier, ; Galván et al, ; Guffanti, Bornstein, & Krulwich, ; Hempfling & Hertzberg, ; Kohlstaedt, Buschmann, Langer, Xie, & Michel, ; Kohlstaedt et al, ; Melin et al, ; Schmetterer et al, ; Sun, Benlekbir et al, ; Sun, Luo et al, ). At the same time, the cbb 3 ‐Cox is only in bacteria and is the sole Cox in pathogenic bacteria.…”

Section: Discussionmentioning

confidence: 99%

The regulation of oxidative phosphorylation pathway on Vibrio alginolyticus adhesion under adversities

Huang

Zhao

et al. 2019

MicrobiologyOpen

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Vibrio alginolyticus is one of the most important pathogens in mariculture and leading to heavy losses. After treatment with Cu2+, Pb2+, and low pH, the expression of oxidative phosphorylation pathway genes, including coxA, coxB, coxC, ccoN, ccoO, and ccoQ, was found commonly downregulated by RNA‐seq as well as quantitative real‐time PCR. RNAi significantly reduced the expression of coxA, coxB, coxC, ccoN, ccoO, and ccoQ in V. alginolyticus. Compared with the wild‐type strain, the adhesion abilities of RNAi strains of V. alginolyticus were significantly impaired, as well as their cytochrome C oxidase activity. ccoQ appeared to be more important in the regulation of bacterial adhesion in these target genes, while ccoO was relatively weak in the regulation of the adhesion. Meanwhile, the changes of temperature, salinity, pH, and starvation affected coxA, coxB, coxC, ccoN, ccoO, and ccoQ expression remarkably. These findings indicated that: the oxidative phosphorylation pathway is a critical regulator of adhesion in V. alginolyticus; coxA, coxB, coxC, ccoN, ccoO, and ccoQ regulate the bacterial adhesion in response to environmental changes such as temperature, salinity, pH, and starvation.

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Section: Discussionmentioning

confidence: 99%

The regulation of oxidative phosphorylation pathway on Vibrio alginolyticus adhesion under adversities

Huang

Zhao

et al. 2019

MicrobiologyOpen

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“…The cytochrome bo 3 complex predominates in growth conditions where oxygen tension is high (Chepuri et al 1990). The enzyme consists of four subunits and has three redox cofactors, a low-spin heme b, a high-spin heme o 3 , and Cu B , all located in subunit I. Heme b is the primary electron acceptor of ubiquinol, while heme o 3 and Cu B form a binuclear active centre where O 2 chemistry occurs (Melin et al 2018). As previously thought, Cytochrome bo3 contains only one ubiquinol binding site located on subunit I instead of two, known as the high-a nity QH site.…”

Section: Unique Genesmentioning

confidence: 99%

Comparative genomic analysis and genome sequence of Halomonas salifodinae strain A2, isolated from the Zapotitlán Salinas Valley Puebla, México

León-Lemus,

-García,

Cabirol

et al. 2024

Preprint

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Here, we report the genome sequence of strain A2. The genome size was 3,855,926 bp, the GC content was 67.4%, and it contains 3509 genes, 62 tRNA, eight rRNA, and four snRNA. Phylogenetic analysis of the 16 S rRNA gene in the RDP, NCBI, and TYGS databases indicates that strain A2 belongs to Halomonas salifodinae. Also, MLSA analysis confirms that A2 is closely related to H. salifodinae. Phylogenomic and comparative genomic analysis using the ANIs and dDDH indicators classify H. salifodinae A2 and Bisbaumannia pacifica NBRC 102220 in a separate phylogenetic group of the genus Halomonas. The phylogenomic and pangenome analysis support the above, placing H. salifodinae A2 in a separate group with B. pacifica NBRC 102220. The pangenomic analysis shows 136,122 genes that comprise the pangenome with 317 core genes, 3457 shell genes, 132,332 accessory genome, and 691 unique genes. We found 29 genes for secretion systems in the genome analysis, 23 for Na + and K + ion transport, 6 BGC groups, a total of 12 genomic islands, an 8.2Kb gene prophage region, 15 regions associated with CRISPR and one CAS-TypeIF cas gene cluster region, 12 genes of biotechnological importance, 38 unique genes essential for adaptability and biotechnological relevance, as well as, 35 genes for the synthesis of compatible solutes. Furthermore, we propose the reclassification of the species within the genus Bisbaumannia.

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“…In contrast to the electron transport chain of mammals that is unbranched, E. coli , like many other prokaryotes, possesses the branched aerobic respiratory chain ( Figure 7 ) [ 45 , 97 , 98 , 99 , 100 , 101 , 102 ]. The E. coli chain comprises of type I and type II NADH dehydrogenases which transfer electrons from NADH to ubiquinol-8 (UQ8) or menaquinol-8 (MQ8); succinate dehydrogenase transferring electrons from succinate to UQ8; and three terminal oxidases, cytochromes bo 3 , bd -I, and bd -II which transfer electrons from UQ8 or MQ8 to O 2 producing H 2 O [ 103 , 104 , 105 , 106 , 107 , 108 , 109 , 110 , 111 , 112 ]. The proton motive force generated by type I NADH dehydrogenase and the terminal oxidases is used by F o F 1 -ATP synthase to make ATP [ 113 , 114 , 115 ].…”

Section: Effect Of H 2 S On the Operation Of The Branched Respiratory Chain Of E Coli And Bacterialmentioning

confidence: 99%

Impact of Hydrogen Sulfide on Mitochondrial and Bacterial Bioenergetics

Borisov

Forte

2021

IJMS

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This review focuses on the effects of hydrogen sulfide (H2S) on the unique bioenergetic molecular machines in mitochondria and bacteria—the protein complexes of electron transport chains and associated enzymes. H2S, along with nitric oxide and carbon monoxide, belongs to the class of endogenous gaseous signaling molecules. This compound plays critical roles in physiology and pathophysiology. Enzymes implicated in H2S metabolism and physiological actions are promising targets for novel pharmaceutical agents. The biological effects of H2S are biphasic, changing from cytoprotection to cytotoxicity through increasing the compound concentration. In mammals, H2S enhances the activity of FoF1-ATP (adenosine triphosphate) synthase and lactate dehydrogenase via their S-sulfhydration, thereby stimulating mitochondrial electron transport. H2S serves as an electron donor for the mitochondrial respiratory chain via sulfide quinone oxidoreductase and cytochrome c oxidase at low H2S levels. The latter enzyme is inhibited by high H2S concentrations, resulting in the reversible inhibition of electron transport and ATP production in mitochondria. In the branched respiratory chain of Escherichia coli, H2S inhibits the bo3 terminal oxidase but does not affect the alternative bd-type oxidases. Thus, in E. coli and presumably other bacteria, cytochrome bd permits respiration and cell growth in H2S-rich environments. A complete picture of the impact of H2S on bioenergetics is lacking, but this field is fast-moving, and active ongoing research on this topic will likely shed light on additional, yet unknown biological effects.

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Role of the tightly bound quinone for the oxygen reaction of cytochrome bo₃ oxidase from Escherichia coli

Cited by 9 publications

References 53 publications

The regulation of oxidative phosphorylation pathway on Vibrio alginolyticus adhesion under adversities

The regulation of oxidative phosphorylation pathway on Vibrio alginolyticus adhesion under adversities

Comparative genomic analysis and genome sequence of Halomonas salifodinae strain A2, isolated from the Zapotitlán Salinas Valley Puebla, México

Impact of Hydrogen Sulfide on Mitochondrial and Bacterial Bioenergetics

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