STUDIES ON COORDINATION CHEMISTRY OF HYDROXAMIC ACID COMPLEXES

Abstract

The present paper process the coordination of monohydroxamic acids to several Zn(II)- or Ni(II)- containing metalloenzymes has been studied by X-ray crystallography. Hydroxamic acids have been long known to inhibit urease, a dinuclear Ni(II)-containing enzyme, which catalyses the hydrolysis of urea to ammonia and carbamate. In the X-ray crystal structure of ahaH (1−)-bound urease from Bacillus pasteurii, the amidohydroxylato group of the acetohydroxamato ligand bridges between the two Ni(II) atoms in the dinuclear active site, which replaces a bridging hydroxyl group in native urease.