β-lactamases, such as the class D β-lactamase OXA-66 expressed by Acinetobacter baumanii, hydrolyze β-lactam antibiotics and play a major role in the antibiotic resistance crisis. To carry out 19F NMR experiments on OXA-66 and thereby better understand its structure and ligand binding, the seven tryptophans of OXA-66 were biosynthetically labeled with fluorine at each tryptophan using various isomers of fluoroindole. The effects of boronic acid inhibitor binding on the 19F NMR spectrum were explored as a function of the position at which the tryptophan was labeled, and resonances were assigned by individually mutating each tryptophan.

19F NMR as a probe of inhibitor binding to β-lactamase OXA-66

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