Spatial relationships between the amine binding site and the copper in plasma amine oxidase

Porcine plasma amine oxidase was covalently modified with a series of fluorine containing phenylhydrazine inhibitors. One mole of phenylhydrazine modifies one mole of enzyme at the amine substrate binding site. NMR relaxation measurements on the fluorine nuclei were obtained at two field strengths for each inhibitor-enzyme complex. These measurements were used to calculate the exact distance and spatial orientation between the inhibitor binding site and the copper cofactor. The copper lies in the plane of the aromatic ring of the inhibitor 10.9, 14.3, and 15.5 A from the ortho-, meta-, and para-positions of the ring, respectively. Since the inhibitors react with the active carbonyl cofactor, this defines the spatial relationship between the copper and the active carbonyl cofactor in the enzyme