The Interaction of Ferric Ions with Jack Bean Urease by Isothermal Titration Calorimetry

Abstract

The aim of the investigations was to measure the influence of Fe 3? ion on jack bean urease (JBU) activity. Interaction between Fe 3? and JBU, is examined using isothermal titration calorimetry. It was found that Fe 3? ions acted as a non-cooperative inhibitor of JBU, and there is a set of 12 identical and independent binding sites for Fe 3? ions. The small structural parameters show that there are little changes on the JBU structure, indicating that Fe 3? has minor effect on the JBU activity. The association equilibrium constant is 42,484.13 ± 110 mol l-1 , indicating the moderate interaction of Fe 3? ion with JBU. The molar enthalpy of binding is DH =-4.33 kJ mol-1 .

Molecular dynamics simulations, molecular docking, and kinetics study of kaempferol interaction on Jack bean urease: Comparison of extended solvation model

“…Meanwhile, the total binding free energy obtained from ITC and extended solvation model was almost close to the MMPBSA result, as shown in Table 2 and 3. Finally, comparing the results of MD with the previous study, it can be seen that the solubility extended solvation model (Behbehani et al, 2009;Behbehani et al, 2016;Behbehani & Barzegar, 2013;Poursoleiman et al, 2019;Rezaei Behbehani, Saboury, Mohebbian, et al, 2010). On many enzymes and inhibitors used in vitro is a successful model that, along with molecular dynamics and simulation, can help researchers in medicine and enzymes and physicians and patients.…”