Models for metal-sulfur coordination in copper proteins.
The oxidation state of copper in several model compounds containing copper coordinated to sulfur, some of which are suggested model compounds for naturally occurring Cu-S chromophores, was determined employing x-ray photoelectron spectrometry. Copper was found to be present in a 3d10 state, which is characteristic for Cu(I). An initial photoreduction is excluded, as Cu(ethylenediamine)2 (SCN)2, in which a Cu-S bond is also present, was found to contain Cu(II) (3d9). As was the case with native parsley plastocyanin, the model compounds reacted effectively with superoxide anion radicals. We suggest that the electrons of the metal-sulfur chromophore in blue copper proteins are delocalized and that an equilibrium: RS--Cu(II) in equilibrium or formed from RS.Cu(I) exists.
D003300:Copper; D003579:Cytochrome Reductases; D008667:Metalloproteins; D008954:Models, Biological; D010084:Oxidation-Reduction; D013052:Spectrometry, X-Ray Emission; D013455:Sulfur; D013482:Superoxide Dismutase / Q000378:metabolism
D008667:Metalloproteins; D013455:Sulfur; D003300:Copper; D013482:Superoxide Dismutase; D003579:Cytochrome Reductases