Abstract
UV-vis absorption spectroscopy has been used to analyze the interaction of myoglobin (Мb) and gallic acid (GA). The binding constants (4.38 × 104 M–1 at 298.15 K and 0.42 × 104 М–1 at 308.15K), the number of binding sites (h = 1.0), and the thermodynamic parameters of binding (ΔH, ΔS, and ΔG) have been determined. Hydrogen bonds have been shown to play a major role in the stabilization of the GA–Мb complexes. GA binding led to slight changes in the electronic state of the heme ring of the protein.
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