| Summary: | This research investigates the molecular level interactions between jack bean urease enzyme and flavone as an inhibitor. It is important to understand how flavone interacts with the active site of urease to inhibit the enzyme’s activity. In this work, the interaction between urease enzyme and flavone inhibitor was examined out using semiempirical quantum mechanical theoretical investigations. Between the two nickels (labelled Ni88 and Ni89), flavone showed tendency to attach to Ni89, where the structure of the inhibitor was distorted to create more positive interactions with the surrounding atoms. The overall interactions, based on the Wiberg Bond Order, show that flavone is able to form stable complexes with urease. It was also found that the interaction energy of -1.52 eV and -1.87 eV for flavone as inhibitor are weaker than urea as adsorbate. Furthermore, the interaction is analyzed not to be that of covalent nature. Hence flavone’s potential as an urease inhibitor is proven theoretically. © 2023 UMT Press. All Rights Reserved.
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