For the viral M pro enzyme, the compounds demonstrated similar stabilities within the active sites of the native and variant enzymes. For the native M pro , the investigated Zn6S6 and Zn6O6 had an intermolecular energy variation between the ground and excited states of 48.33 kcal mol -1 for Zn6S6 and 48.25 kcal mol -1 for Zn6O6. For the mutant M pro , these variations were 48.99 kcal mol -1 for Zn6S6 and 52.79 kcal mol -1 for Zn6O6. The stability of the compounds Zn6S6 and Zn6O6 in the mutant M pro active site was similar to that of the native enzyme. Thus, our findings suggest that these compounds may also act on this variant. According to the results computed for the cutinase of Fusarium solani, the interaction energies demonstrated a stabilizing effect, as supported by the favourable values of interaction energy obtained, similar to the results of M pro of SARS-CoV-2. The interaction energy of Zn6S6 and Zn6O6 was also stabilising when targeting the DNA gyrase of Escherichia coli. However, the interaction of the excited state of Zn6O6 cluster was more stabilising for DNA gyrase than for cutinase. Trends regarding the interaction modes of these compounds were observed for both the ground and excited states, and in all cases, both Zn6S6 and Zn6O6 presented more stabilising interactions in the excited site.