A Model for the Inhibition of Urease by Hydroxamates

摘要

The structure of a nickel hydroxamate complex is presented which gives new insight for the mechanism of hydroxamate-based inhibition of dinuclear hydrolytic enzymes. These results show that the possibility of a hydroxamate bridging the two nickel atoms in urease is reasonable and that the properties of such an inhibited form are consistent with the accumulated physical data. Furthermore, as illustrated by enolase and aminopeptidases, inhibition of enzymes with dinuclear active centers by hydroxamates may generally rely on such bridging structures.