Transition from octahedral to tetrahedral geometry causes the activation or inhibition by Zn2+ of Pseudomonas aeruginosa phosphorylcholine phosphatase

OTERO, LH; BEASSONI, PR; LISA, AT; DOMENECH, CE

BIOMETALS

SPRINGER

Año: 2010 vol. 23 p. 307 - 314

0966-0844

Pseudomonas aeruginosa phosphorylcholine phosphatase (PchP) catalyzes the hydrolysis of phosphorylcholine, which is produced by the action of hemolytic phospholipase C on phosphatidylcholine or sphyngomielin, to generate choline and inorganic phosphate. Among divalent cations, its activity is dependent on Mg2+ or Zn2+. Mg2+ produced identical activation at pH 5.0 and 7.4, but Zn2+ was an activator at pH 5.0 and became an inhibitor at pH 7.4. At this higher pH, very low concentrations of Zn2+ inhibited enzymatic activity even in the presence of saturating Mg2+ concentrations. Considering experimental and theoretical physicochemical calculations performed by different authors, we conclude that at pH 5.0, Mg2+ and Zn2+ are hexacoordinated in an octahedral arrangement in the PchP active site. At pH 7.4, Mg2+ conserves the octahedral coordination maintaining enzymatic activity. The inhibition produced by Zn2+ at 7.4 is interpreted as a change from octahedral to tetrahedral coordination geometry which is produced by hydrolysis of the Zn2L1 2 L0 2  H2O2[1] complex