Growth of an mutant deficient in respiration

Futatsugi, Lui; Saito, Hidehiko; Kakegawa, Tomohito; Kobayashi, Hisao

doi:10.1016/s0378-1097(97)00417-5

Cited by 16 publications

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“…It is likely that Fdh‐H and Hyd‐4 combine to form a second FHL system (FHL‐2) in E. coli that is driven by the proton gradient established by F 0 F 1 ‐ATPase. The physiological purpose of the FHL‐2 pathway is uncertain, but it may be required for the generation of CO 2 during fermentation at high pH (above pH ∼7) [26] for use in the generation of oxalate by phosphoenolpyruvate carboxylase that in turn could be used for biosynthesis or for the consumption of reducing equivalents and for H 2 ‐dependent fumarate respiration. FHL‐1 and FHL‐2 would appear to have distinct functions during fermentation.…”

Section: Discussionmentioning

confidence: 99%

The roles of hydrogenases 3 and 4, and the F₀F₁‐ATPase, in H₂ production by Escherichia coli at alkaline and acidic pH

et al. 2002

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The hyc operon of Escherichia coli encodes the H 2 -evolving hydrogenase 3 (Hyd-3) complex that, in conjunction with formate dehydrogenase H (Fdh-H), constitutes a membrane-associated formate hydrogenlyase (FHL) catalyzing the disproportionation of formate to CO 2 and H 2 during fermentative growth at low pH. Recently, an operon (hyf) encoding a potential second H 2 -evolving hydrogenase (Hyd-4) was identified in E. coli. In this study the roles of the hyc-and hyf-encoded systems in formate-dependent H 2 production and Fdh-H activity have been investigated. In cells grown on glucose under fermentative conditions at slightly acidic pH the production of H

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Section: Discussionmentioning

confidence: 99%

The roles of hydrogenases 3 and 4, and the F₀F₁‐ATPase, in H₂ production by Escherichia coli at alkaline and acidic pH

et al. 2002

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“…E. coli is able to grow at a low pH, for instance below 6.0 [14–16], when the cytoplasmic pH is lowered and transport systems might be changed. It has been shown that the rate of K + uptake through TrkA under aerobic conditions is strongly decreased with lowering the external and cytoplasmic pH by a weak acid [17].…”

Section: Introductionmentioning

confidence: 99%

Kup is the major K⁺ uptake system in Escherichia coli upon hyper‐osmotic stress at a low pH

Trchоunian

Kobayashi

1999

FEBS Letters

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The K + uptake was observed in washed cells of Escherichia coli, wild-type, upon hyper-osmotic stress at pH 5.5 when glucose was supplemented. This uptake had apparent a K m of 0.58 mM and V mx of 0.10 W Wmol K + /min/mg protein. Such a K + uptake was investigated using a mutant defective in Kdp and TrkA but with a functional Kup and a mutant defective in Kdp and Kup but having an active TrkA. The K + uptake to reach the steady state level as well as the initial K + influx rate in the first mutant were at least 3.5-fold greater than these values with the second mutant and similar to those of the wild-type. Such differences in the K + uptake activity were correlated with K + requirements for growth of these mutants. Moreover, the K + uptake in the wild-type was blocked by a protonophore (carbonyl cyanide m-chlorophenylhydrazone). Valinomycin, arsenate and N,NP-dicyclohexylcarbodiimide were not effective in changing the K + uptake. It is suggested that Kup is the major K + uptake system in E. coli upon hyper-osmotic stress at a low pH.z 1999 Federation of European Biochemical Societies.

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Novel insights into the bioenergetics of mixed-acid fermentation: Can hydrogen and proton cycles combine to help maintain a proton motive force?

Trchоunian

Sawers

2013

IUBMB Life

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Escherichia coli possesses four [NiFe]-hydrogenases that catalyze the reversible redox reaction of 2H(+) + 2e(-) ↔ H2. These enzymes together have the potential to form a hydrogen cycle across the membrane. Their activity, operational direction, and interaction with each other depend on the fermentation substrate and particularly pH. The enzymes producing H2 are likely able to translocate protons through the membrane. Moreover, the activity of some of these enzymes is dependent on the F0 F1 -ATPase, thus linking a proton cycle with the cycling of hydrogen. These two cycles are suggested to have a primary basic role in modulating the cell's energetics during mixed-acid fermentation, particularly in response to pH. Nevertheless, the mechanisms underlying the physical interactions between these enzyme complexes, as well as how this is controlled, are still not clearly understood. Here, we present a synopsis of the potential impact of proton-hydrogen cycling in fermentative bioenergetics.

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Growth of an mutant deficient in respiration

Cited by 16 publications

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The roles of hydrogenases 3 and 4, and the F₀F₁‐ATPase, in H₂ production by Escherichia coli at alkaline and acidic pH

The roles of hydrogenases 3 and 4, and the F₀F₁‐ATPase, in H₂ production by Escherichia coli at alkaline and acidic pH

Kup is the major K⁺ uptake system in Escherichia coli upon hyper‐osmotic stress at a low pH

Novel insights into the bioenergetics of mixed-acid fermentation: Can hydrogen and proton cycles combine to help maintain a proton motive force?

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Growth of an mutant deficient in respiration

Cited by 16 publications

References 0 publications

The roles of hydrogenases 3 and 4, and the F0F1‐ATPase, in H2 production by Escherichia coli at alkaline and acidic pH

The roles of hydrogenases 3 and 4, and the F0F1‐ATPase, in H2 production by Escherichia coli at alkaline and acidic pH

Kup is the major K+ uptake system in Escherichia coli upon hyper‐osmotic stress at a low pH

Novel insights into the bioenergetics of mixed-acid fermentation: Can hydrogen and proton cycles combine to help maintain a proton motive force?

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The roles of hydrogenases 3 and 4, and the F₀F₁‐ATPase, in H₂ production by Escherichia coli at alkaline and acidic pH

The roles of hydrogenases 3 and 4, and the F₀F₁‐ATPase, in H₂ production by Escherichia coli at alkaline and acidic pH

Kup is the major K⁺ uptake system in Escherichia coli upon hyper‐osmotic stress at a low pH