Computational Studies of Ion Pairing. 10. Ion Pairing between Tetrabutylammonium ion and Inorganic Ions: A General Motif Confirmed

2015 ◽  
Vol 80 (8) ◽  
pp. 3758-3765 ◽  
Author(s):  
Albert J. Fry
Molecules ◽  
2020 ◽  
Vol 25 (2) ◽  
pp. 303
Author(s):  
Abderrahman Atifi ◽  
Michael D. Ryan

Understanding the solvation and ion-pairing interactions of anionic substrates in room-temperature ionic liquids (RTIL) is key for the electrochemical applications of these new classes of solvents. In this work, cyclic voltammetry and visible and infrared spectroelectrochemistry of tetracyanoquinodimethane (TCNQ) was examined in molecular (acetonitrile) and RTIL solvents, as well as mixtures of these solvents. The overall results were consistent with the formation of RTIL/acetonitrile nanodomains. The voltammetry indicated that the first electrogenerated product, TCNQ−, was not incorporated into the RTIL nanodomain, while the second electrogenerated product, TCNQ2−, was strongly attracted to the RTIL nanodomain. The visible spectroelectrochemistry was also consistent with these observations. Infrared spectroelectrochemistry showed no discrete ion pairing between the cation and TCNQ− in either the acetonitrile or RTIL solutions. Discrete ion pairing was, however, observed in the acetonitrile domain between the tetrabutylammonium ion and TCNQ2−. On the other hand, no discrete ion pairing was observed in BMImPF6 or BMImBF4 solutions with TCNQ2−. In BMImNTf2, however, discrete ion pairs were formed with BMIm+ and TCNQ2−. Density function theory (DFT) calculations showed that the cations paired above and below the aromatic ring. The results of this work support the understanding of the redox chemistry in RTIL solutions.


Author(s):  
Ronald D. Edstrom ◽  
Xiuru Yang ◽  
Mary E. Gurnack ◽  
Marcia A. Miller ◽  
Rui Yang ◽  
...  

Many of the questions in biochemistry and cell biology are concerned with the relationships of proteins and other macromolecules in complex arrays which are responsible for carrying out metabolic sequences. The simplistic notion that the enzymes we isolate in soluble form from the cytoplasm were also soluble in vivo is being replaced by the concept that these enzymes occur in organized systems within the cell. In this newer view, the cytoplasm is organized and the “soluble enzymes” are in fact fixed in the cellular space and the only soluble components of the cell are small metabolites, inorganic ions etc. Further support for the concept of metabolic organization is provided by the evidence of metabolic channeling. It has been shown that for some metabolic pathways, the intermediates are not in free diffusion equilibrium with the bulk liquid in the cell but are passed along, more or less directly, from one enzyme to the next.


1977 ◽  
Vol 86 (3) ◽  
pp. 552-560 ◽  
Author(s):  
Monica Söderberg ◽  
Inge-Bert Täljedal

ABSTRACT Effects of inorganic ions on the uptake of chloromercuribenzene-p-sulphonic acid (CMBS) were studied in microdissected pancreatic islets of non-inbred ob/ob-mice. Na2SO4 stimulated the total islet cell uptake of CMBS but decreased the amount of CMBS remaining in islets after brief washing with L-cysteine. CaCl2 stimulated both the total and the cysteine-non-displaceable uptake; the stimulatory effect of CaCl2 on the cysteine-non-displaceable CMBS uptake was counteracted by Na2SO4. NaCl, KCl or choline chloride had no significant effect on the total islet cell uptake of CMBS, whereas LiCl was stimulatory. It is concluded that β-cells resemble erythrocytes in having a permeation path for CMBS that is inhibited by SO42−. By analogy with existing models of the erythrocyte membrane, it is suggested that the SO42−-sensitive path leads to sulphydryl groups controlling monovalent cationic permeability in β-cells.


2005 ◽  
Author(s):  
David A. Forsyth ◽  
Okan Arikan ◽  
Leslie Ikemoto ◽  
James O'Brien ◽  
Deva Ramanan

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