Computational study of the structure and catalytic mechanism of xylene monooxygenase from Pseudomonas putida

Xylene monooxygenase (XMO) from Pseudomonas putida stands out for its ability to oxidize inert substrates with a structure like toluene and xylene. Nevertheless, its catalytic efficacy is curtailed by a mysterious inhibition mechanism, the details of which remain elusive. Presently, our research endeavors focus on employing wet and computational methodologies to unravel the structural intricacies and catalytic dynamics of XMO atoms. This enzyme exhibits high sequence homology with alkane monooxygenase (alkB), with its distinctive catalytic site where two iron atoms are situated at an unusual distance of 6 Å within a histidine-rich environment. This peculiar catalytic site underlines a catalytic mechanism unknown to this day. While our investigation is ongoing, our preliminary molecular modeling and simulation efforts aim to shed light on the fundamental aspects of its function and inhibition. Through this ongoing work, we anticipate laying the groundwork for potential strategies to enhance the stability and efficiency of XMO. Our endeavors hold significant promise for advancing both the fundamental understanding and practical applications of XMO in biotechnological contexts such as industrial processes.