Association of triethanolamine and related ligands with alkali metal ions and ion pairs in tetrahydrofuran at 25.degree.C

1976 ◽  
Vol 80 (7) ◽  
pp. 679-685 ◽  
Author(s):  
H. B. Flora ◽  
W. R. Gilkerson
Keyword(s):  
Alkali Metal ◽  
Metal Ions ◽  
Ion Pairs ◽  
Alkali Metal Ions

Metal ion catalysis in nucleophilic displacement reactions at carbon, phosphorus, and sulfur centers. III. Catalysis vs. inhibition by metal ions in the reaction of p-nitrophenyl benzenesulfonate with ethoxide

1990 ◽  
Vol 68 (10) ◽  
pp. 1846-1858 ◽  
Author(s):  
Marko J. Pregel ◽  
Edward J. Dunn ◽  
Erwin Buncel
Keyword(s):  
Alkali Metal ◽  
Transition State ◽  
Metal Ions ◽  
Ground State ◽  
Rate Constants ◽  
Metal Ion ◽  
Ion Pairs ◽  
Alkali Metal Ions ◽  
Complexing Agent ◽  
Metal Ion Catalysis

The rate of the nucleophilic displacement reaction of p-nitrophenyl benzenesulfonate (1) with alkali metal ethoxides in ethanol at 25 °C has been studied by spectrophotometric techniques. For lithium ethoxide, sodium ethoxide, potassium ethoxide, and cesium ethoxide, the observed rate constants increase in the order LiOEt < NaOEt < CsOEt < KOEt. The effect of added crown ether and cryptand complexing agents was also investigated. Addition of complexing agent to the reaction of KOEt results in the rate decreasing to a minimum value corresponding to the reaction of free ethoxide. Conversely, addition of complexing agent to the reaction of LiOEt results in the rate increasing to a maximum value that is identical to the minimum value seen in the reaction of KOEt in the presence of excess complexing agent. In complementary experiments, alkali metal ions were added in the form of unreactive salts. Addition of a K+ salt to the reaction of KOEt increases the reaction rate, while addition of a Li+ salt to the reaction of LiOEt decreases the rate. The involvement of metal ions in the reaction of 1 is proposed to occur via reactive alkali metal – ethoxide ion pairs. The kinetic data are analyzed in terms of an ion pairing treatment that allows the calculation of second-order rate constants for free ethoxide and metal–ethoxide ion pairs; the rate constants increase in the order LiOEt < EtO−< NaOEt < CsOEt < KOEt. Thus, Li+isaninhibitorofthereactionofethoxidewith1, whiletheothermetalsionsstudiedareallcatalysts. Equilibrium constants for the association of the various metal ions with the transition state are calculated using a thermodynamic cycle, and are compared to association constants in the ground state. Consistent with the observed kinetic results, Li+ is found to stabilize the ground state more than the transition state, while Na+, K+, and Cs+ all stabilize the transition state more than the ground state. The trend in the magnitude of the transition state stabilization is interpreted in terms of interactions of the transition state with bare or solvated metal ions. It is concluded that the transition state for the reaction of 1 with ethoxide forms solvent separated ion pairs with alkali metal ions. Analogous data were available for the reaction of p-nitrophenyl diphenylphosphinate (2) with ethoxides, where Li+, Na+, K+, and Cs+ all function as catalysts, and the results are analyzed as above. In contrast to the sulfonate system, it is proposed that the phosphinate transition state forms contact ion pairs with alkali metal ions. The difference is attributed to a greater localization of negative charge in the phosphinate transition state, leading to stronger interactions with metal ions, which overcome metal ion – solvent interactions. Keywords: nucleophilic substitution at sulfur, alkali metal ion catalysis.

Ion–peptide interactions between alkali metal ions and a termini-protected dipeptide: modeling a portion of the selectivity filter in K+ channels

2019 ◽  
Vol 21 (2) ◽  
pp. 561-571 ◽  
Author(s):  
Shun-ichi Ishiuchi ◽  
Yuta Sasaki ◽  
James M. Lisy ◽  
Masaaki Fujii
Keyword(s):  
Alkali Metal ◽  
Metal Ions ◽  
Selectivity Filter ◽  
Alkali Metal Ions ◽  
K Channels ◽  
Peptide Interactions

Differentiating K+ and Na+ binding patterns in peptide sequences.

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