N-Hydroxyurea binds both to carbonic anhydrase (CA) and to matrix
metalloproteinases (MMPs). X-ray crystallography showed N-hydroxyurea to bind in
a bidentate mode by means of the oxygen and nitrogen atoms of the NHOH moiety to
the Zn(II) ion of CA, participating in a network of hydrogen bonds with a water
molecule and Thr199. A derivatized N-hydroxyurea showed low-micromolar affinity
for several CAs. This simple zinc binding function may be exploited for
obtaining potent metalloenzyme inhibitors, due to its versatility of binding to
the metal ion present in the active site of such enzymes.