Proton conductance and regulation of proton/potassium fluxes in Escherichia coli FhlA-lacking cells during fermentation of mixed carbon sources
Escherichia coli uptake potassium ions with the coupling of proton efflux and energy utilization via proton FOF1-ATPase. In this study contribution of formate hydrogen lyase (FHL) complexes in the proton/potassium fluxes and the formation of proton conductance (CMH+) were investigated using fhlA mut...
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Veröffentlicht in: | Archives of biochemistry and biophysics 2024-05, Vol.755, p.109999-109999, Article 109999 |
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Sprache: | eng |
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Zusammenfassung: | Escherichia coli uptake potassium ions with the coupling of proton efflux and energy utilization via proton FOF1-ATPase. In this study contribution of formate hydrogen lyase (FHL) complexes in the proton/potassium fluxes and the formation of proton conductance (CMH+) were investigated using fhlA mutant strain. The proton flux rate (JH+) decreased in fhlA by ∼ 25 % and ∼70 % during the utilization of glucose and glycerol, respectively, at 20 h suggesting H+ transport via or through FHL complexes. The decrease in JK+ in fhlA by ∼40 % proposed the interaction between FHL and Trk secondary transport system during mixed carbon fermentation. Moreover, the usage of N,N′-dicyclohexylcarbodiimide (DCCD) demonstrated the mediation of FOF1-ATPase in this interaction. CMH+ was 13.4 nmol min−1 mV−1 in WT at 20 h, which decreased by 20 % in fhlA. Taken together, FHL complexes have a significant contribution to the modulation of H+/K+ fluxes and the CMH + for efficient energy transduction and regulation of the proton motive force during mixed carbon sources fermentation.
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•JH + decreased in fhlA by ∼25 % and ∼70 % at 20 h.•CMH+ was 13.4 nmol min−1 mV−1 in WT at 20 h, which decreased by 20 % in fhlA.•FHL complexes have significant contribution in the modulation of H+/K+ fluxes and the CMH+. |
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ISSN: | 0003-9861 1096-0384 |
DOI: | 10.1016/j.abb.2024.109999 |