Evidence for hydrogenase-4 catalyzed biohydrogen production in Escherichia coli

Mirzoyan, S. Å.; Romero, P.; Oviedo, María Dolores Coello; Trchоunian, Armen; Trchounian, Karen

doi:10.1016/j.ijhydene.2017.07.126

Cited by 29 publications

(12 citation statements)

References 48 publications

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“…As it was stated, the interaction between proton ATPase and different membrane‐bound systems is possible directly or indirectly depending on external conditions such as pH, redox potential, carbon source etc. Usually under fermentative conditions, it has been shown that interaction between different membrane‐bound enzymes or proteins such as the F O F 1 ‐ATPase and Trk or the F O F 1 ‐ATPase and Hyd takes place directly via interprotein dithiol‐disulfide intechange (‐SH‐HS to –S‐S) for conserving energy and maintaining ΔpH and thus proton motive force …”

Section: Resultsmentioning

confidence: 99%

“…Usually under fermentative conditions, it has been shown that interaction between different membranebound enzymes or proteins such as the F O F 1 -ATPase and Trk or the F O F 1 -ATPase and Hyd takes place directly via interprotein dithiol-disulfide intechange (-SH-HS to -S-S) for conserving energy and maintaining ΔpH and thus proton motive force. 12,29,31,32 3.2 | DCCD-inhibited ATPase activity and number of SH groups at pH 5.5 in E. coli wild type and FDH deficient mutants…”

Section: Others Reagents and Data Processingmentioning

confidence: 99%

“…The second FHL complex is composed of FDH-H and Hyd-4. 8 The activity of Hyd-4 is suggested under different conditions [10][11][12] but still it has not been purified and biochemically characterized. Recently, Finney et al 13 characterized functional FHL-2 complex in plant pathogen Pectobacterium atrosepticum.…”

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: Resultsmentioning

confidence: 99%

Section: Others Reagents and Data Processingmentioning

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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“…In contrast, the quinone-dependent pyruvate dehydrogenase (PoxB), which could transfer electrons generated upon pyruvate fermentation to menaquinone, is downregulated in fermenting cells and therefore most likely does not contribute significantly to pyruvate oxidation under this condition. A pyruvate formate lyase is not encoded in any Sulfurospirillum spp., which, in addition to the low protein abundance of a cytoplasmic formate dehydrogenase in S. multivorans and S. cavolei , argues against the role of the Hyf in an FHL complex as opposed to the suggested function for Hyf in E. coli 32 . The generated acetyl-CoA is used to generate acetate and one mol ATP per mol pyruvate via substrate-level phosphorylation.…”

Section: Discussionmentioning

confidence: 95%

“…The putative H 2 -producing, cytoplasmically oriented enzyme (Hyf) is a large, complex enzyme with eight subunits, four of them presumably membrane-integral. Regarding amino acid sequence and subunit architecture, this hydrogenase is similar to hydrogenase 4 of Escherichia coli , part of a putative second formate hydrogen lyase (FHL) 32 . However, in S. multivorans , Hyf is unlikely to form an FHL complex since the corresponding gene cluster does not encode any formate-specific proteins as is the case for the FHL complexes in E. coli (Supplementary Figure 1 ).…”

Section: Introductionmentioning

confidence: 98%

Hydrogen production by Sulfurospirillum species enables syntrophic interactions of Epsilonproteobacteria

et al. 2018

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Hydrogen-producing bacteria are of environmental importance, since hydrogen is a major electron donor for prokaryotes in anoxic ecosystems. Epsilonproteobacteria are currently considered to be hydrogen-oxidizing bacteria exclusively. Here, we report hydrogen production upon pyruvate fermentation for free-living Epsilonproteobacteria, Sulfurospirillum spp. The amount of hydrogen produced is different in two subgroups of Sulfurospirillum spp., represented by S. cavolei and S. multivorans. The former produces more hydrogen and excretes acetate as sole organic acid, while the latter additionally produces lactate and succinate. Hydrogen production can be assigned by differential proteomics to a hydrogenase (similar to hydrogenase 4 from E. coli) that is more abundant during fermentation. A syntrophic interaction is established between Sulfurospirillum multivorans and Methanococcus voltae when cocultured with lactate as sole substrate, as the former cannot grow fermentatively on lactate alone and the latter relies on hydrogen for growth. This might hint to a yet unrecognized role of Epsilonproteobacteria as hydrogen producers in anoxic microbial communities.

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Impaired glucose metabolism by deleting the operon of hydrogenase 2 in Escherichia coli

Shekhar

Maeda²

2022

Arch Microbiol

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Evidence for hydrogenase-4 catalyzed biohydrogen production in Escherichia coli

Cited by 29 publications

References 48 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 by Sulfurospirillum species enables syntrophic interactions of Epsilonproteobacteria

Impaired glucose metabolism by deleting the operon of hydrogenase 2 in Escherichia coli

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