The Interaction of Coumarin Antibiotics with Fragments of the DNA Gyrase B Protein

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Abstract
DNA gyrase is the target of the coumarin group of antibacterial agents. The drugs are known to inhibit the ATPase activity of gyrase and bind to the 24-kDa N-terminal subdomain of the gyrase B protein. Supercoiling assays with intact DNA gyrase and ATPase assays with a 43-kDa N-terminal fragment of the B protein suggest that the drugs bind tightly, with Kd values 105 M-1·s-1, and dissociation rate constants of ∼3 × 10-3 s-1 and ∼4 × 10-3 s-1 for the 43- and 24-kDa proteins, respectively. Titration calorimetry shows that the Kd values for coumarins binding to both proteins are ∼10-8 M and that binding is enthalpy driven.

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