During pyruvate oxidation in anaerobic bacteria, pyruvate ferredoxin oxidoreductase (PFOR) converts pyruvate to Acetyl-CoA with the cofactor thiamine pyrophosphate (TPP). Amixcile, a derivative of a previously established drug nitazoxanide (NTZ), is a drug that prevents pyruvate from binding to PFOR and thus halts pyruvate oxidation. This study thus utilizes docking simulations to virtually observe and compare NTZ and amixcile’s interaction with PFOR. It was observed that the propylamine tail in amixicile allowed for interaction with more amino acid residues in the active site of PFOR, along with other key interactions.