Assignment of a ligand in stellacyanin by a pulsed electron paramagnetic resonance method.

The electron spin echo decay envelope for the blue copper protein, stellacyanin, and for a number of other Cu(II) complexes has been studied. Particular attention was given to the form of the "nuclear modulation" patterns, which show the effects of coupling between the electron spin and the neighboring nuclei. The envelopes for the hydrated cupric complex and for copper(II) glycylglycine were essentially the same and indicative of the coupling to protons. The peptide complex contains nitrogen nuclei coupled directly to Cu(II), but the coupling constant is so large for these nuclei that a modulation pattern ascribable to 14N is not seen. For copper(II) bovine serum albumin, on the other hand, a contribution due to the coupling of the remote nitrogen belonging to a histidyl imidazole ligand was observed. The modulation pattern for this complex and for stellacyanin closely resembled one another, strongly suggesting that an imidazole is ligated to the copper in this blue protein.