Abstract
1. Introduction The metalloprotein erythrocuprein has been known for 35 years [ 11, but the discovery of its enzymatic function by McCord and Fridovich [2] as a dismutase of superoxide radicals has occurred only 30 years after. More recently evidence has been produced that singlet oxygen is produced in biological systems [3-61, and that SOD’, besides its dismutase activity, is capable of transforming singlet oxygen to ground state triplet oxygen [7,8 1. Some reports, however, did not confirm the proposed ‘singlet oxygen decontaminase’ activity of the enzyme [lo-121. The problem has been reinvestigated by studying the effect of SOD on the peroxidation of linoleic acid by lipoxidase. This reaction, in fact, has been demonstrated to yield as an intermediate only O2 * and not superoxide radicals [4,10,11]. Thus an inhibition of linoleic acid peroxidation by SOD would be indicative that this enzyme can catalyze singlet to triplet oxygen transformation. Moreover, since Oa * has a half life of 2 psec in Ha 0 [ 141, but ten-fold as high in Da 0 [ 151, it is expected that a more pronounced inhibition of SOD would be visible
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