Insights into molecular metabolism of herbicide-resistant CYP81As through molecular docking and MM/GBSA analysis

The structural protein of heme-containing monooxygenases, the CYP81As family, was modeled and evaluated in terms of herbicide-resistant study. A molecular docking study revealed the possible binding conformation of QC/CYP81As. The molecular mechanism of QC in complex with CYP81As suggests that CYP81A12 could be the preferential protein target for the QC metabolite, which is congruent with the experimental study. Additionally, the essential binding amino acid and the influence of HEME for QC/CYP81As have been proposed through per-residue decomposition free energy calculation using the MM/GBSA method. The possible metabolism of QC is elucidated through the combination of experimental and computational studies.