Electron-Nuclear Double Resonance of a Protein That Contains Copper: Evidence for Nitrogen Coordination to Cu(II) in Stellacyanin

Abstract
Electron-nuclear double resonance has been used to study ligand hyperfine interactions of the copper (II) complex in a frozen solution of the blue protein stellacyanin. It is shown that the copper ion coordinates with at least one nitrogen ligand, and probably more than one, and that the copper ion is in a hydrophobic environment.