Energy transduction by electron transfer via a pyrrolo-quinoline quinone-dependent glucose dehydrogenase in Escherichia coli, Pseudomonas aeruginosa, and Acinetobacter calcoaceticus (var. lwoffi)

Abstract

The coupling of membrane-bound glucose dehydrogenase (EC 1.1.99.17) to the respiratory chain has been studied in whole cells, cell-free extracts, and membrane vesicles of gram-negative bacteria. Several Escherichia coil strains synthesized glucose dehydrogenase apoenzyme which could be activated by the prosthetic group pyrrolo-quinoline quinone. The synthesis of the glucose dehydrogenase apoenzyme was independent of the presence of glucose in the growth medium. Membrane vesicles of E. coli, grown on glucose or succinate, oxidized glucose to gluconate in the presence of pyrrolo-quinoline quinone. This oxidation led to the generation of a proton motive force which supplied the driving force for uptake of lactose, alanine, and glutamate. Reconstitution of glucose dehydrogenase with limiting amounts of pyrrolo-quinoline quinone allowed manipulation of the rate of electron transfer in membrane vesicles and whole cells. At saturating levels of pyrrolo-quinoline quinone, glucose was the most effective electron donor in E. coli, and glucose oxidation supported secondary transport at even higher rates than oxidation of reduced phenazine methosulfate. Apoenzyme of pyrrolo-quinoline quinone-dependent glucose dehydrogenases with similar properties as the E. coli enzyme were found in Acinetobacter calcoaceticus (var. Iwoffi) grown aerobically on acetate and in Pseudomonas aeruginosa grown anaerobically on glucose and nitrate.on July 5, 2020 by guest http://jb.asm.org/ Downloaded from 494 van SCHIE ET AL.

Evidence for mutualism between a plant growing in a phosphate-limited desert environment and a mineral phosphate solubilizing (MPS) rhizobacterium

“…A bioenergetic role for the direct oxidation pathway has been shown for some bacterial genera [10], however in other bacteria it has not been possible to attribute an essential physiological role for this pathway giving rise to the term`dissimilatory bypass'. For example, a P. cepacia mutant lacking glucose dehydrogenase activity was isolated by Lessie et al [11].…”

The Entner-Doudoroff pathway: history, physiology and molecular biology

“…Thus, phosphate limitation leads indirectly to induction of the Entner-Doudoroff pathway. Oxidative glucose metabolism may indeed provide a bioenergetic advantage in the environment, since it is found in a large number of enteric and free-living, aquatic microorganisms [45]. It seems reasonable that E. coli should be able to harness the energy of electron transfer via PQQ-dependent glucose dehydrogenase, which is supported by the finding that growth on glucose plus PQQ results in higher cell yields than growth on glucose alone [41].…”

Ca2+ and its Substitutes have Two Different Binding Sites and Roles in Soluble, Quinoprotein (Pyrroloquinoline‐Quinone‐Containing) Glucose Dehydrogenase

“…Given the broad spectrum of bivalent metal ions effective in reconstituting quinoprotein dehydrogenase apoenzymes to active holoenzymes, but the limited spectrum for an individual enzyme, the specificity is not so much determined by PQQ but by the variable metal-ion-binding sites.The bacterium Acinetobacter calcoaceticus produces two quite different PQQ-containing (quinoprotein) glucose dehydrogenases, the membrane-bound enzyme (mGDH) and the soluble enzyme (sGDH). mGDH occurs in many gram-negative bacteria [l] and glucose oxidation via this enzyme provides the organism with useful energy [2]. The deduced amino acid sequence of this Correspondence to J.…”

“…The bacterium Acinetobacter calcoaceticus produces two quite different PQQ-containing (quinoprotein) glucose dehydrogenases, the membrane-bound enzyme (mGDH) and the soluble enzyme (sGDH). mGDH occurs in many gram-negative bacteria [l] and glucose oxidation via this enzyme provides the organism with useful energy [2]. The deduced amino acid sequence of this Correspondence to J.…”