Ion transfer at the interface between an aqueous solution in the presence of concentrated salts and an organic solution studied by polarography at the electrolyte solution dropping electrode

Ogura, Kaoru; Kihara, Sorin; Suzuki, Mitsuko; Matsui, Masanao

doi:10.1016/0022-0728(93)80260-o

Cited by 5 publications

(2 citation statements)

References 32 publications

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“…We showed that the Δ W W ′ G ° values for ClO 4 − , Et 4 N + , or Me 4 N + are not affected by the concentration of hydrophilic polymers added in aqueous solution. , This suggests that these appreciably bulky ions can be utilized as references for the calculation of Δ W W ′ G ° j of a single ionic species. Similar trends for these ions were confirmed in concentrated salt solutions . Δ W W ′ G ° j can thus be derived by Δ W W ′ G ° j = z j F ΔΔ E I = 0 …”

Section: Resultssupporting

confidence: 68%

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Perturbation of Second and Farther Hydration Shells of Alkali Cations and Bromide in Concentrated Aqueous Protein as a Water-Shortage Medium

2008

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The Gibbs free energies of transfer of selected ions from water to concentrated aqueous ovalbumin and albumin (DeltaW(W') G degrees j) have been determined by ion-transfer voltammetry. Negative values for the tetrabutylammonium ion suggest its direct binding to ovalbumin. In contrast, for alkali cations and bromide, the DeltaW(W') G degrees j values are positive and increase with increasing ovalbumin concentration. Positive values are confirmed for concentrated aqueous albumin and poly(styrenesulfonate) as well. The largest value (ca. 10 kJ mol(-1)) is found for the transfer of K(+) from water to 30 wt % ovalbumin. To reveal the solvation structure of these ions in ovalbumin solutions, X-ray absorption fine structure (XAFS) measurements have been performed at the K, Rb, and Br K-edges. Interestingly, the spectra obtained in 30 wt % ovalbumin solutions are identical to those for the corresponding hydrated ions. This strongly suggests that the first coordination shell structures of these ions are not affected by a large concentration of ovalbumin. The detected positive free energy of transfer is slightly lower than the hydrogen bonding energy of a water molecule and should thus come from the perturbation of the second and farther hydration shells of the ions under a water-shortage condition caused by a high concentration of ovalbumin.

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Section: Resultssupporting

confidence: 68%

“…Similar trends for these ions were confirmed in concentrated salt solutions. 22 ∆ W W′ G°j can thus be derived by…”

Section: Resultsmentioning

confidence: 99%

Perturbation of Second and Farther Hydration Shells of Alkali Cations and Bromide in Concentrated Aqueous Protein as a Water-Shortage Medium

2008

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Regular Irregularity in the Transfer of Anionic Surfactant across the Liquid/Liquid Interface

et al. 2003

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Irregular current spikes and other anomalies seen in voltammetry of the transfer of anionic surfactants, alkyl sulfonates, and alkyl sulfates across the 1,2-dichloroethane/water (DCE/W) interface are reproducible. The anomalies have a certain regularity that is predicted by a recently proposed concept, the electrochemical instability. Irregular current spikes follow after the augmentation of the current induced when the phase-boundary potential is brought close to the mid-point potential of the transferring surfactant ions. Potential-step chronoamperometry clearly demonstrates the presence of the instability window, that is, the potential region where the interface becomes unstable only in the limited range of the phase-boundary potential.

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Charge transfer processes on liquid/liquid interfaces: The first century

Vanýsek

1995

Electrochimica Acta

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Ion transfer at the interface between an aqueous solution in the presence of concentrated salts and an organic solution studied by polarography at the electrolyte solution dropping electrode

Cited by 5 publications

References 32 publications

Perturbation of Second and Farther Hydration Shells of Alkali Cations and Bromide in Concentrated Aqueous Protein as a Water-Shortage Medium

Perturbation of Second and Farther Hydration Shells of Alkali Cations and Bromide in Concentrated Aqueous Protein as a Water-Shortage Medium

Regular Irregularity in the Transfer of Anionic Surfactant across the Liquid/Liquid Interface

Charge transfer processes on liquid/liquid interfaces: The first century

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