Exploring particulate methane monooxygenase (pMMO) proteins using experimentation and computational molecular docking

Researchers had difficulty studying pure full-length pMMO due to the solubility problem and loss of enzymatic activity after its elimination from the native membrane. To study pMMO, we performed sev-eral bioinformatics tools to analyze the entire structure of it available in the PDB database. We also car-ried out molecular docking studies to prove that quinone and duroquinone can bind to several sites of eight pMMO proteins. However, some sites in the orientation are not required by the catalysis process. Furthermore, molecular docking was done for predicting the binding affinity of P450 with target enzymes. Interestingly, our analysis illustrated that pMMO can produce methanol in the presence of qui-none and duroquinone and the absence of Cu. Moreover, pmoB1 can interact with P450. Consequently, our findings highlight, for the first time, the significance of studying the membrane of pMMO to provide valuable insights into its functions.(c) 2023 The Author(s). Published by Elsevier B.V. on behalf of King Saud University. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

Automated summary

Researchers used bioinformatics tools and molecular docking studies to analyze the structure of pMMO and its interactions with quinone, duroquinone, and P450 enzymes. They discovered that pMMO can produce methanol without Cu in the presence of quinone and duroquinone, and that pmoB1 interacts with P450. This study highlights the importance of studying the membrane of pMMO for understanding its functions.