Spectroscopic characterization of copper(II) thermolysin
Abstract
The compound obtained from zinc-free thermolysin and copper(II) sulphate, which is biologically inactive, has been characterized together with some inhibitor derivatives of the native enzyme through electronic, e.s.r., and n.m.r. spectroscopies. The co-ordination at the metal is suggested to be pseudo-tetrahedral. A comparison with the similar copper(II)-substituted metalloenzyme carboxypeptidase is presented.