X-ray Absorption Fine Structure (XAFS) experiments have been performed
to probe detailed structural changes at the active site of carboxypep
tidase A (ZnCPD) from neutral to alkaline pHs. Direct comparison and a
nalysis on the first coordination shells of ZnCPD revealed structural
differences between pH 7.0 and pH 9.9. The observed structural changes
indicated that one of the ligands to the metal moves to a 0.09 angstr
om shorter distance from the zinc ion at the alkaline pH, resulting in
a shorter metal-ligand distance and an increased first shell structur
al disorder. Such a situation would be expected if the water ligand of
the zinc ion was converted to hydroxide at the alkaline pH.