Reactions between Mercuric Mercury and Cysteine and Glutathione. Apparent Dissociation Constants, Heats and Entropies of Formation of Various Forms of Mercuric Mercapto-Cysteine and -Glutathione
Biochemical analysis demonstrates thermodynamic parameters of mercuric cysteine and glutathione complexes, indicating high-affinity heavy metal coordination.
Key Points
To determine the chemical equilibria, apparent dissociation constants, and thermodynamic properties of formation for complexes between mercuric mercury and cysteine or glutathione.
Measured stoichiometric reactions between mercuric mercury ions and sulfur-containing biomolecules (cysteine and glutathione).
Calculated thermodynamic values including apparent dissociation constants, enthalpies (heats), and entropies of formation across distinct complex forms.
Identified and characterized multiple coordination states of mercuric mercapto-cysteine and mercuric mercapto-glutathione complexes.
Quantified the thermodynamic stability, dissociation constants, and energetic formation profiles governing mercuric-thiol binding.