Binding of Au(CN)2- and Pt(CN)4-2- to horse liver alcohol dehydrogenase. A 35C1NMR relaxation study.

The study investigated how Au(CN)2- and Pt(CN)4-2- ions bind to the coenzyme binding site of horse liver alcohol dehydrogenase, using 35C1 nuclear magnetic relaxation. Analysis of the relaxation rates helped estimate binding constants for these ions and enabled the researchers to derive estimations for the correlation time and quadrupole coupling constant of a bound chloride ion.

Objective of the research

• The study aims to explore and understand how Au(CN)2- and Pt(CN)4-2- ions bind to the coenzyme binding site of horse liver alcohol dehydrogenase.
• This understanding is gleaned from analysis using 35C1 nuclear magnetic relaxation.

Methodology

• Using 35C1 nuclear magnetic relaxation, the research evaluated the longitudinal relaxation rates.
• These rates were then analyzed using a simple model for determining the binding constants for the ions Au(CN)2-, Pt(CN)4-2-, and Cl-.

Key findings

• The study derived estimations for binding constants for the ions Au(CN)2-, Pt(CN)4-2-, and Cl-.
• Furthermore, through a comparison between transverse and longitudinal relaxation rates, estimations were made for the correlation time and quadrupole coupling constant of a bound chloride ion.

Conclusion

• From a simple electrostatic model for a chloride ion interacting with an arginine group, the quadrupole coupling constant was evaluated which concurred with the experimental value.
• This exploration offers insights into the interaction specific ions have with the coenzyme binding site of horse liver alcohol dehydrogenase, potentially aiding future pharmacological and biochemistry research.