Impact of membrane-associated hydrogenases on the FOF1-ATPase in Escherichia coli during glycerol and mixed carbon fermentation: ATPase activity and its inhibition by N,N′-dicyclohexylcarbodiimide in the mutants lacking hydrogenases

Blbulyan, Syuzanna; Trchоunian, Armen

doi:10.1016/j.abb.2015.05.015

Cited by 30 publications

(43 citation statements)

References 40 publications

(89 reference statements)

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“…The ATPase activity was expressed in nmol P i (min μg protein) −1 . P i was determined spectrophotometrically (UV–VIS spectrophotometer, Cary 60, Agilent Technologies) by the method, as described . The DCCD‐inhibited ATPase activity was calculated as a difference between activities in the absence and in the presence of the inhibitor.…”

Section: Methodsmentioning

confidence: 99%

“…Note, ATP can reach ATPase in right-side-out MVs due to membrane peculiarities of cells grown under the mentioned conditions or the presence of in-side-out MVs in the preparations, as suggested. 18 The ATPase activity was expressed in nmol P i (min μg protein) −1 . P i was determined spectrophotometrically (UV-VIS spectrophotometer, Cary 60, Agilent Technologies) by the method, as described.…”

Section: Atpase and Accessible Sh-groups Assaysmentioning

confidence: 99%

“…16,17 In addition, recently it was shown that during mixed carbon (glucose and glycerol) sources fermentation DCCDinhibited proton ATPase activity depends also on Hyd enzymes. 18,19 During single-carbon source (glucose or glycerol) fermentative conditions, role of different Hyd enzymes, proton ATPase, formate dehydrogenase activities is generally described. 1,[18][19][20] However, in natural environments, Enterobacterium spp.…”

Section: Introductionmentioning

confidence: 99%

“…18,19 During single-carbon source (glucose or glycerol) fermentative conditions, role of different Hyd enzymes, proton ATPase, formate dehydrogenase activities is generally described. 1,[18][19][20] However, in natural environments, Enterobacterium spp. such as E. coli always encounters complex mixtures of carbon sources.…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Methodsmentioning

confidence: 99%

Section: Atpase and Accessible Sh-groups Assaysmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

2019

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“…The intracellular pH and, hence, proton-motive force were lower at pH 7.5 compared with those during glucose fermentation [50]. Proton motive force generation is changed in E. coli hypF mutant lacking all Hyd enzymes [50] due to the effects on the F O F 1 -ATPase too [52]. Therefore, Hyd impact on an overall proton-motive force generation is disclosed; H + pumping by Hyd is suggested.…”

Section: Hydrogenases For Hydrogen Production By E Coli During Glycementioning

confidence: 95%

Hydrogen production from glycerol by Escherichia coli and other bacteria: An overview and perspectives

Trchounian

Trchоunian

2015

Applied Energy

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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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Impact of membrane-associated hydrogenases on the FOF1-ATPase in Escherichia coli during glycerol and mixed carbon fermentation: ATPase activity and its inhibition by N,N′-dicyclohexylcarbodiimide in the mutants lacking hydrogenases

Cited by 30 publications

References 40 publications

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

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

Hydrogen production from glycerol by Escherichia coli and other bacteria: An overview and perspectives

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

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Impact of membrane-associated hydrogenases on the FOF1-ATPase in Escherichia coli during glycerol and mixed carbon fermentation: ATPase activity and its inhibition by N,N′-dicyclohexylcarbodiimide in the mutants lacking hydrogenases

Cited by 30 publications

References 40 publications

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

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

Hydrogen production from glycerol by Escherichia coli and other bacteria: An overview and perspectives

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

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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