Prolongation of H2 production during mixed carbon sources fermentation in E. coli batch cultures: New findings and role of different hydrogenases

Mirzoyan, S. Å.; Vassilian, Anait; Trchоunian, Armen; Trchounian, Karen

doi:10.1016/j.ijhydene.2018.03.189

Cited by 16 publications

(10 citation statements)

References 53 publications

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“…In addition, H 2 production in batch cultures was monitored during ~240 h in hybC mutant . In hycE mutant which has defect in large subunit of Hyd‐3 (component of FHL‐1 complex) no any H 2 production was detected in batch cultures which is in good conformity with our results with the mutants where selC gene is absent (coding for FDH‐H also which is component of FHL‐1 complex): again no any H 2 production was measured in H 2 production assays . Interestingly, at pH 7.5 and pH 6.5 DCCD did not affect H 2 production in all assays (see Fig.…”

Section: Resultssupporting

confidence: 87%

“…It has been described that when E. coli cells were grown in batch cultures in the presence of mixture of glucose, glycerol and formate in the same concentrations as used in this study, wild type cells yielded 8.8 mmol H 2 per L of medium and in hybC (defect in large subunit of Hyd‐2) mutant H 2 production yield has been increased by approximately 1.6‐fold compared to wild type cells. In addition, H 2 production in batch cultures was monitored during ~240 h in hybC mutant . In hycE mutant which has defect in large subunit of Hyd‐3 (component of FHL‐1 complex) no any H 2 production was detected in batch cultures which is in good conformity with our results with the mutants where selC gene is absent (coding for FDH‐H also which is component of FHL‐1 complex): again no any H 2 production was measured in H 2 production assays .…”

Section: Resultssupporting

confidence: 87%

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Understanding the Role of Escherichia coli Hydrogenases and Formate Dehydrogenases in the F_OF₁‐ATPase Activity during the Mixed Acid Fermentation of Mixture of Carbon Sources

2018

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During fermentation Escherichia coli produces di-hydrogen (H ) via reversible membrane-bound [Ni-Fe]-hydrogenases (Hyd). This study describes the total and N,N'-dicyclohexylcarbodiimide (DCCD) inhibited ATPase activity and H production at various pHs in E. coli wild type and mutants encoding Hyd enzymes and formate dehydrogenases (FDH) on fermentation of glucose, glycerol, and formate. The highest total ATPase activity was detected at pH 7.5 in hyaB hybC selC (lacking large subunits of Hyd-1 and Hyd-2 and FDH, respectively) triple mutant. This ATPase activity was mainly due to the proton-translocating ATPase but in FDH mutant the DCCD inhibition was less compared to wild type. Potassium ions stimulated total ATPase activity at pH 5.5 ~50% and ~35% in wild type and hypF (lacking all Hyd enzymes) mutant, respectively. Moreover, K also stimulated DCCD inhibited ATPase activity ~1.7-fold-2-fold in strains where FDH was absent only at pH 5.5. DCCD inhibited H production only at pH 5.5 in all assays. Taken together it is suggested that at low pH, FDH, and Hyd enzymes are linked with the F F -ATPase for regulating and maintaining the cytoplasmatic pH and thus proton motive force generation. FDH and Hyd enzymes have impact on the F F -ATPase activity depending on external pH and potassium ions. © 2018 IUBMB Life, 70(10):1040-1047, 2018.

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Section: Resultssupporting

confidence: 87%

Section: Resultssupporting

confidence: 87%

Understanding the Role of Escherichia coli Hydrogenases and Formate Dehydrogenases in the F_OF₁‐ATPase Activity during the Mixed Acid Fermentation of Mixture of Carbon Sources

2018

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“…It is already well known that E. coli can ferment not only single but also mixtures of carbon sources . Especially, when glucose and/or glycerol were fermented totally and DCCD‐inhibited ATPase activity was highest at pH 7.5 …”

Section: Resultsmentioning

confidence: 99%

“…3 | RESULTS AND DISCUSSION 3.1 | DCCD-inhibited ATPase activity and number of SH groups at pH 7.5 in E. coli wild type and FDH deficient mutants It is already well known that E. coli can ferment not only single but also mixtures of carbon sources. [33][34][35] Especially, when glucose and/or glycerol were fermented totally and DCCD-inhibited ATPase activity was highest at pH 7.5. 18,19 When E. coli wild type cells were grown during fermentation of glucose, glycerol, and formate, total ATPase activity was~182 nmol P i (min μg protein) −1 .…”

Section: Others Reagents and Data Processingmentioning

confidence: 99%

Formate and potassium ions affect Escherichia coli proton ATPase activity at low pH during mixed carbon fermentation

2019

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Escherichia coli is able to ferment not only single but also mixtures of carbon sources. The formate metabolism and effect of formate on various enzymes have been extensively studied during sole glucose but not mixed carbon sources utilization. It was revealed that in membrane vesicles (MV) of wild type cells grown at pH 7.5 during fermentation of the mixture of glucose (2 g/L), glycerol (10 g/L), and formate (0.68 g/L), in the assays, the addition of formate (10 mM) increased the N,N′‐dicyclohexylcarbodiimide (DCCD)‐inhibited ATPase activity on ~30% but no effect of potassium ions (100 mM) had been detected. In selC (coding formate dehydrogenases) and fdhF (coding formate dehydrogenase H) single mutants, formate increased DCCD‐inhibited ATPase activity on ~40 and ~70%, respectively. At pH 5.5, in wild type cells MV, formate decreased the DCCD‐inhibited ATPase activity ~60% but unexpectedly in the presence of potassium ions, it was stimulated ~5.8 fold. The accessible SH or thiol groups number in fdhF mutant was less by 28% compared with wild type. In formate assays, the available SH groups number was less ~10% in wild type but not in fdhF mutant. Taken together, the data suggest that proton ATPase activity depends on externally added formate in the presence of potassium ions at low pH. This effect might be regulated by the changes in the number of redox‐active thiol groups via formate dehydrogenase H, which might be directly related to proton ATPase FO subunit.

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“…External formate added as a carbon substrate is utilized by bacteria (~2.6 mM) during bacterial growth lag phase at pH 7.5, but H 2 generation was not determined. 38 The absence of absorbance of external formate in fhlA mutant cells is presumably due to the lack of enzymes that break down the formate, and the cells did not assimilate what could not be oxidized or is bioenergetically less or non-favorable. 41 Formate as a weak organic acid can dissipate proton motive force.…”

Section: Discussionmentioning

confidence: 99%

The role of Escherichia coli FhlA transcriptional activator in generation of proton motive force and F_OF₁‐ATPase activity at pH 7.5

et al. 2021

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Escherichia coli is able to utilize the mixture of carbon sources and produce molecular hydrogen (H 2 ) via formate hydrogen lyase (FHL) complexes. In current work role of transcriptional activator of formate regulon FhlA in generation of fermentation end products and proton motive force, N 0 N 0dicyclohexylcarbodiimide (DCCD)-sensitive ATPase activity at 20 and 72 hr growth during utilization of mixture of glucose, glycerol, and formate were investigated. It was shown that in fhlA mutant specific growth rate was~1.5 fold lower compared to wt, while addition of DCCD abolished the growth in fhlA but not in wt. Formate was not utilized in fhlA mutant but wt cells simultaneously utilized formate with glucose. Glycerol utilization started earlier (from 2 hr) in fhlA than in wt. The DCCD-sensitive ATPase activity in wt cells membrane vesicles increased~2 fold at 72 hr and was decreased 70% in fhlA. Addition of formate in the assays increased proton ATPase activity in wt and mutant strain. FhlA absence mainly affected the ΔpH but not ΔΨ component of Δp in the cells grown at 72 hr but not in 24 hr. The Δp in wt cells decreased from 24 to 72 hr of growth~40 mV while in fhlA mutant it was stable. Taken together, it is suggested that FhlA regulates the concentration of fermentation end products and via influencing F O F 1 -ATPase activity contributes to the proton motive force generation.

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Prolongation of H2 production during mixed carbon sources fermentation in E. coli batch cultures: New findings and role of different hydrogenases

Cited by 16 publications

References 53 publications

Understanding the Role of Escherichia coli Hydrogenases and Formate Dehydrogenases in the F_OF₁‐ATPase Activity during the Mixed Acid Fermentation of Mixture of Carbon Sources

Understanding the Role of Escherichia coli Hydrogenases and Formate Dehydrogenases in the F_OF₁‐ATPase Activity during the Mixed Acid Fermentation of Mixture of Carbon Sources

Formate and potassium ions affect Escherichia coli proton ATPase activity at low pH during mixed carbon fermentation

The role of Escherichia coli FhlA transcriptional activator in generation of proton motive force and F_OF₁‐ATPase activity at pH 7.5

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Prolongation of H2 production during mixed carbon sources fermentation in E. coli batch cultures: New findings and role of different hydrogenases

Cited by 16 publications

References 53 publications

Understanding the Role of Escherichia coli Hydrogenases and Formate Dehydrogenases in the FOF1‐ATPase Activity during the Mixed Acid Fermentation of Mixture of Carbon Sources

Understanding the Role of Escherichia coli Hydrogenases and Formate Dehydrogenases in the FOF1‐ATPase Activity during the Mixed Acid Fermentation of Mixture of Carbon Sources

Formate and potassium ions affect Escherichia coli proton ATPase activity at low pH during mixed carbon fermentation

The role of Escherichia coli FhlA transcriptional activator in generation of proton motive force and FOF1‐ATPase activity at pH 7.5

Contact Info

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Resources

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Understanding the Role of Escherichia coli Hydrogenases and Formate Dehydrogenases in the F_OF₁‐ATPase Activity during the Mixed Acid Fermentation of Mixture of Carbon Sources

Understanding the Role of Escherichia coli Hydrogenases and Formate Dehydrogenases in the F_OF₁‐ATPase Activity during the Mixed Acid Fermentation of Mixture of Carbon Sources

The role of Escherichia coli FhlA transcriptional activator in generation of proton motive force and F_OF₁‐ATPase activity at pH 7.5