Abstract Polycyclic aromatic hydrocarbons (PAHs) are organic, liposoluble compounds generated by incomplete combustion and commonly found in the environment, causing damage to both ecosystems and humans. Bioremediation is a biological process that removes contaminants from the environment, thereby reducing these damages. This study aimed to perform in silico analyses to investigate the effectiveness of the enzyme Catechol 1,2-dioxygenase from Pseudomonas aeruginosa in degrading certain polycyclic aromatic hydrocarbons (PAHs), which are absorbed by and harmful to the human body. The objective was to evaluate the biodegradation potential of PAHs by Catechol 1,2-dioxygenase, an enzyme involved in the PAH degradation pathway, to obtain data on its activity when isolated from the bacterial microenvironment. A three-dimensional structural model of Catechol 1,2-dioxygenase was obtained through molecular modeling, and this model was evaluated by molecular docking to assess its interaction with several PAHs: naphthalene, anthracene, and pyrene. The enzyme formed complexes with all tested PAHs, with pyrene, a highly carcinogenic compound in humans, showing the highest affinity for the enzyme from P. aeruginosa. These findings suggest that the enzyme exhibits activity outside the bacterial microenvironment; however, its potential for in situ application requires further in vitro studies.
Geraldo et al. (Wed,) studied this question.