Anhydrous proton transport system based on zwitterionic liquid and HTFSI

2004 ◽  
pp. 1828 ◽  
Author(s):  
Masahiro Yoshizawa ◽  
Hiroyuki Ohno
Keyword(s):  
Transport System ◽  
Proton Transport ◽  
Anhydrous Proton Transport

scholarly journals Hierarchical Porous Polybenzimidazole Microsieves: An Efficient Architecture for Anhydrous Proton Transport via Polyionic Liquids

2017 ◽  
Vol 9 (17) ◽  
pp. 14844-14857 ◽  
Author(s):  
Parashuram Kallem ◽  
Martin Drobek ◽  
Anne Julbe ◽  
Erik J. Vriezekolk ◽  
Reyes Mallada ◽  
...  
Keyword(s):  
Proton Transport ◽  
Hierarchical Porous ◽  
Anhydrous Proton Transport

L-Malate transport and proton symport in vesicles prepared from Pseudomonas putida

1986 ◽  
Vol 64 (11) ◽  
pp. 1190-1194 ◽  
Author(s):  
F. R. Agbanyo ◽  
G. Moses ◽  
N. F. Taylor
Keyword(s):  
Membrane Potential ◽  
Pseudomonas Putida ◽  
Kinetic Analysis ◽  
Transport System ◽  
Electron Donor ◽  
Proton Transport ◽  
Proton Motive Force ◽  
Alkaline Ph ◽  
Proton Symport ◽  
Malate Transport

In vesicles from glucose-grown Pseudomonas putida, L-malate is transported by nonspecific physical diffusion. L-Malate also acts as an electron donor and generates a proton motive force (Δp) of 129 mV which is composed of a membrane potential (Δψ) of 60 mV and a ΔpH of 69 mV. In contrast, vesicles from succinate-grown cells (a) transport L-malate by a carrier-mediated system with a Km value of 14.3 mM and a Vmax of 313 nmol∙mg protein−1∙min−1, (b) generate no Δψ, ΔpH, or Δp when L-malate is the electron donor, and (c) produce an extravesicular alkaline pH during the transport of L-malate. A kinetic analysis of this L-malate-induced proton transport gives a Km value of 16 mM and a Vmax of 667 nmol H+∙mg protein−1∙min−1. This corresponds to a H+/L-malate ratio of 2.1. The failure to generate a Δp in these vesicles is considered, therefore, to be consistent with the induction in succinate-grown cells of an electrogenic proton symport L-malate transport system.

scholarly journals Publisher’s Note: Facile Anhydrous Proton Transport on Hydroxyl Functionalized Graphane [Phys. Rev. Lett. 118 , 186101 (2017)]

2017 ◽  
Vol 118 (23) ◽  
Author(s):  
Abhishek Bagusetty ◽  
Pabitra Choudhury ◽  
Wissam A. Saidi ◽  
Bridget Derksen ◽  
Elizabeth Gatto ◽  
...  
Keyword(s):  
Proton Transport ◽  
Anhydrous Proton Transport

scholarly journals Facile Anhydrous Proton Transport on Hydroxyl Functionalized Graphane

2017 ◽  
Vol 118 (18) ◽  
Author(s):  
Abhishek Bagusetty ◽  
Pabitra Choudhury ◽  
Wisssam A. Saidi ◽  
Bridget Derksen ◽  
Elizabeth Gatto ◽  
...  
Keyword(s):  
Proton Transport ◽  
Anhydrous Proton Transport

scholarly journals Transport of galactose, glucose and their molecular analogues by Escherichia coli K12

1977 ◽  
Vol 162 (2) ◽  
pp. 309-320 ◽  
Author(s):  
P J F Henderson ◽  
R A Giddens ◽  
M C Jones-Mortimer
Keyword(s):  
Escherichia Coli ◽  
Transport System ◽  
Proton Transport ◽  
Regulatory Mechanism ◽  
Transport Systems ◽  
British Library ◽  
Transport Activity ◽  
Phosphotransferase System ◽  
Escherichia Coli K12 ◽  
Specific Transport System

1. Strains of Escherichia coli K12 were made that are unable to assimilate glucose by the phosphotransferase system, since they lack the glucose-specific components specified by the genes ptsG and ptsM. 2. Derivative organisms lacking the methyl galactoside or galactose-specific transport system were examined for their ability to transport galactose, d-fucose, methyl beta-D-galactoside, glucose, 2-deoxy-D-glucose and methyl alpha-D-glucoside. 3. Galactose, glucose and to a lesser extent fucose are substrates for both transport systems. 4. 2-Deoxyglucose is transported on the galactose-specific but not the methyl galactoside system. 5. The ability of sugars to elicit anaerobic proton transport is associated with the galactose-specific, but not with the methyl galactoside transport activity. Hence a chemiosmotic mechanism of energization is likely to apply to the former but not to the latter. Alternatively the methyl galactoside system may be switched off under certain conditions, which would indicate a novel regulatory mechanism. 6. Details of the procedure for the derivation of strains may be obtained from the authors, and have been deposited as Supplementary Publication SUP 50074 (8 pages at the) British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1977), 161,1.

scholarly journals Na+/Ca2+ exchange in coated microvesicles

1986 ◽  
Vol 233 (3) ◽  
pp. 643-648 ◽  
Author(s):  
T Saermark ◽  
M Gratzl
Keyword(s):  
Enzyme Activity ◽  
Atpase Activity ◽  
Kinetic Analysis ◽  
Transport System ◽  
Proton Transport ◽  
Ion Accumulation ◽  
Secretory Vesicles ◽  
Proton Permeability ◽  
Total Capacity

Coated microvesicles isolated from bovine neurohypophyses could be loaded with Ca2+ in two different ways, either by incubation in the presence of ATP or by imposition of an outwardly directed Na+ gradient. Na+, but not K+, was able to release Ca2+ accumulated by the coated microvesicles. These results suggest the existence of an ATP-dependent Ca2+-transport system as well as of a Na+/Ca2+ carrier in the membrane of coated microvesicles similar to that present in the membranes of secretory vesicles from the neurohypophysis. A kinetic analysis of transport indicates that the apparent Km for free Ca2+ of the ATP-dependent uptake was 0.8 microM. The average Vmax. was 2 nmol of Ca2+/5 min per mg of protein. The total capacity of microvesicles for Ca2+ uptake was 3.7 nmol/mg of protein. Both nifedipine (10 microM) and NH4Cl (50 mM) inhibited Ca2+ uptake. The ATPase activity in purified coated-microvesicles fractions from brain and neurohypophysis was characterized. Micromolar concentrations of Ca2+ in the presence of millimolar concentrations of Mg2+ did not change enzyme activity. Ionophores increasing the proton permeability across membranes activated the ATPase activity in preparations of coated microvesicles from brain as well as from the neurohypophysis. Thus the enzyme exhibits properties of a proton-transporting ATPase. This enzyme seems to be linked to the ion accumulation by coated microvesicles, although the precise coupling of the proton transport to Ca2+ and Na+ fluxes remains to be determined.

scholarly journals Constructing Straight Polyionic Liquid Microchannels for Fast Anhydrous Proton Transport

2016 ◽  
Vol 8 (51) ◽  
pp. 35377-35389 ◽  
Author(s):  
Parashuram Kallem ◽  
Adela Eguizabal ◽  
Reyes Mallada ◽  
Maria Pilar Pina
Keyword(s):  
Proton Transport ◽  
Polyionic Liquid ◽  
Anhydrous Proton Transport
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