Coordination Studies of the Metal Center of Hemocyanin by 199mHg Nuclear Quadrupole Interaction

The nuclear quadrupole interaction of 1 9 9 m Hg monitored by time differential perturbed angular correlations of γ-rays was employed to investigate the binding of Hg(II) to the binuclear metal site in the copper protein hemocyanin Eurypelma californicum. The data indicate that Hg(II) occupies the two metal sites and alters the metal site geometry from a trigonal to a digonal coordination.