Interactions Of Water-Soluble Zinc Porphyrin With Amino Acids
Inorganica Chimica Acta: Bioinorganic Chemistry
Equilibrium constants for replacement in aqueous solution of the axial ligand of tetrakis(4-N-methyl-pyridyl)porphinezinc(II) by a variety of amino acids at pH 9 have been determined spectrophotometrically. In addition, the equilibrium constant was determined for glycine as a function of pH. From the pH studies, it appears that the substitution of glycine of OH− at the Zn center is thermodynamically less favorable than for replacement of H₂O. Stabilization due to intramolecular non-covalent bonding between side-chains of several L-amino acids and the porphyrin macrocycle has also been observed.
E. Mikros, A. Gaudemer, and Robert F. Pasternack.
"Interactions Of Water-Soluble Zinc Porphyrin With Amino Acids".
Inorganica Chimica Acta: Bioinorganic Chemistry.
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