Characterization of Flavonol Inhibition of DnaB Helicase: Real-Time Monitoring, Structural Modeling, and Proposed Mechanism
Figure 4
ssDNA-dependent ATPase activity of KpDnaB. (a) The vanadate-sensitive colorimetric determination of inorganic phosphate released by the hydrolysis of ATP. A standard linear regression curve was generated by plotting the optical density (OD) at 610 nm against the concentrations of sodium phosphate (NaH2PO4). (b) ATPase activity of KpDnaB is inhibited by flavonols. In the presence of Myr, Que, Kae, or Gal, the specific activity of KpDnaB was decreased to 59%, 75%, 65%, and 57%, respectively.
