Molecular Medical Microbiology 2015
DOI: 10.1016/b978-0-12-397169-2.00011-1
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Bacterial Energy Metabolism

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Cited by 24 publications
(15 citation statements)
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“…Cytochrome bd oxidases, catalyze the two-electron oxidation of either ubiquinol or menaquinol are at the end of the respiratory chain where they couple with the Na + -translocating NADH:quinone oxidoreductase (Na + -NQR) and other dehydrogenases such as NADH-linked lactate dehydrogenase [7174]. The Na + -NQR system also acts as a primary sodium pump and respiratory module at bacterial membrane that mediates electron transfer from NADH to quinone, which is coupled with the translocation of sodium ions across membrane generating a sodium motive force [75, 76] or chemiosmosis [7784]. Here, during growth at the subsurface of soft agar, genes predicted to encode a Na + -NQR system were upregulated.…”
Section: Resultsmentioning
confidence: 99%
“…Cytochrome bd oxidases, catalyze the two-electron oxidation of either ubiquinol or menaquinol are at the end of the respiratory chain where they couple with the Na + -translocating NADH:quinone oxidoreductase (Na + -NQR) and other dehydrogenases such as NADH-linked lactate dehydrogenase [7174]. The Na + -NQR system also acts as a primary sodium pump and respiratory module at bacterial membrane that mediates electron transfer from NADH to quinone, which is coupled with the translocation of sodium ions across membrane generating a sodium motive force [75, 76] or chemiosmosis [7784]. Here, during growth at the subsurface of soft agar, genes predicted to encode a Na + -NQR system were upregulated.…”
Section: Resultsmentioning
confidence: 99%
“…Energy metabolism is vital for physiological processes and biochemical pathways for driving division and cell growth in microbes such as bacteria [ 56 , 57 ]. Interactions in mixed microbial cultures are driven by metabolite exchanges and are dependent on symbiotic and sometimes competitive behaviours [ 58 , 59 ].…”
Section: Discussionmentioning
confidence: 99%
“…Subsequently, the proton motive force is converted to adenosine triphosphate (ATP). The key enzyme, F0F1 ATPase, consists of a hydrophobic F0 component (formed from integral membrane proteins A, B and C) and a hydrophilic F1 component (formed from five subunits α, β, λ, δ and ϵ) (68). According to our results, the expression of the whole F0 component and at least two subunits (δ (SCO5370) and ϵ(SCO5374)) of the F1 component were also found to be controlled by HrdB.…”
Section: Discussionmentioning
confidence: 99%