Abstract
Copper proteins involving either isolated centres (horse liver alcohol dehydrogenase with Cu(II) at the active site, cupric complex of BSA and porcine ceruloplasmin) or binuclear cuprous ( Limulus polyphemus deoxyhemocyanin, Cu(I) complex with disulphides in BSA) or cupric sites ( Limulus deoxymethemocyanin) were studied by means of DPP in buffered media. The reduction of the binuclear sites was directly observable in the polarograms. The reduction responses of the isolated cupric centres were promoted either by EDTA or in a weakly acidic buffered medium at pH 5.4 to 5.6. Electroactive ternary complexes (e.g. Cu(II): protein: EDTA) permitting a bridged electron transfer are proposed to be the key intermediates in the promoted electroreduction of cupric centres.
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