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• W1971999712 abstract "Abstract Phenol—butylamine Schiff base 1:1 systems are studied in methylcyclohexane solutions. The thermodynamic data (Δ H 0 and Δ S 0 ) of the hydrogen bond formation and of the proton transfer in the OH•••N ⇌ O − •••H + N bonds are determined using IR spectroscopy. In all systems studied these hydrogen bonds show large proton polarizability since double-minimum proton potentials are present, whereby the deeper well is at the N. The amounts of the negative Δ H 0 PT and Δ S 0 PT values increase in proportion to the Δp K a (p K a of the protonated Schiff base minus p K a of the phenol). For one phenol—Schiff base system the thermodynamic quantities were determined using a variety of solvents of different polarity. The amounts of the negative Δ H 0 PT and Δ S 0 PT values increase with increasing polarity of the solvent. A retinal Schiff base is the chromophore in visual pigment proteins (rhodopsin and bacteriorhodopsin). On the basis of our experimental results conclusions are presented concerning proton transfer processes between the side group of the amino acid tyrosine (which is a phenolic group) and the retinal Schiff base in the protein." @default.
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• W1971999712 date "1987-10-01" @default.
• W1971999712 modified "2023-10-18" @default.
• W1971999712 title "Influence of phenol acidity and solvent polarity with phenol—retinal schiff base hydrogen bonds—thermodynamic parameters of bond formation and proton transfer" @default.
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• W1971999712 doi "https://doi.org/10.1016/0022-2860(87)85064-0" @default.
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