Water-soluble zinc porphyrins as artificial receptors for amino acids.
The binding of amino acids to water-soluble zinc porphyrins in basic aqueous solution was spectrophotometrically analyzed. The amino acids were bound to the porphyrins through the coordination of the N atom with the central zinc ion. Additional attractions arise due to Coulomb interactions between the -COO(-) anion of the amino acids and the -N(CH(3))(3)(+) cation of the porphyrin substituents and due to hydrophobic interactions between the porphyrin plane and the hydrophobic substituents of the amino acids. These attractions could be explained based on the binding data. The compensatory relationships of DeltaS and DeltaH were also discussed.
Imai
Hiroyasu
H
Faculty of Pharmaceutical Sciences, Hokuriku University, Kanazawa, Japan. h-imai@hokuriku-u.ac.jp
Misawa
Kensuke
K
Munakata
Hiroki
H
Uemori
Yoshio
Y
D000588:Amines / Q000737:chemistry; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D008665:Metalloporphyrins / Q000737:chemistry*; D017459:Receptors, Amino Acid / Q000737:chemistry*; D013816:Thermodynamics
D000588:Amines; D008665:Metalloporphyrins; D017459:Receptors, Amino Acid; C017802:zinc hematoporphyrin