From haemocuprein to copper-zinc superoxide dismutase: a history on the fiftieth anniversary of the discovery of haemocuprein and the twentieth anniversary of the discovery of superoxide dismutase.
Haemocuprein was discovered fifty years ago by T. Mann and D. Keilin as a copper protein of red blood cells, later named erythrocuprein. Superoxide dismutase was discovered twenty years ago by J.M. McCord and I. Fridovich as an enzymatic activity in preparations of carbonic anhydrase or myoglobin that inhibited the aerobic reduction of cytochrome c by xanthine oxidase. Astonishingly the superoxide dismutase proved to be haemocuprein. Around this time zinc was found in haemocuprein, in equimolar amount to the copper. Haemocuprein thus became copper-zinc superoxide dismutase after thirty years as an obscure cuproprotein of red blood cells. This historical article is a tribute to the achievement of J.M. McCord and I. Fridovich. Their discovery of superoxide dismutase revolutionized the study of oxygen free-radicals in biochemistry.
Bannister
W H
WH
Department of Physiology and Biochemistry, University of Malta, Msida.
D000818:Animals; D004912:Erythrocytes / Q000201:enzymology; D006801:Humans; D013482:Superoxide Dismutase / Q000097:blood*
D013482:Superoxide Dismutase