Abstract
Ag I 2 Cu II 2 SOD, a derivative of bovine superoxide dismutase containing Ag and Cu rather than Cu and Zn, has been studied by a wide range of paramagnetic resonance techniques. Evidence based on the linear electric field effect (LEFE) in pulsed EPR supports the original conclusion that Cu(II) occupies the Zn(II) site of the native protein, substantially retaining the pseudo-tetrahedral coordination geometry.
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