Theoretical Insights into the Formation of Oxygen Activation Sites with the Affection of Protein Microenvironment in Flavin-Dependent Monooxygenases Msud

Abstract

Through comprehensive computational methods, the O2 binding as well as the role of the protein microenvironment in MsuD enzyme were investigated. This work identified the O2 binding site in MsuD enzyme and discovered a possible oxygen migration channel within MsuD enzyme. Molecular dynamics simulations after residue mutation proved that residues Asn105 play an important role on maintaining the O2 position. We demonstrated N5 as a favorable reaction site and speculated a reasonable O2 activation process. This work recovers the formation of oxygen activation sites in MsuD enzyme, which is of great significance for further investigations of the catalytic reaction mechanism.

Keywords: Flavin-dependent monooxygenase, MsuD enzyme, Molecular Dynamics, MDpocket