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Hemin degradation was observed in the presence of NADH and lipoamide dehydrogenase at pH 6.5-9.0. The degradation was inhibited by 80% by catalase and by 70% by superoxide dismutase. This system oxidized oxyhemoglobin to methemoglobin but only slightly degraded heme in hemoglobin.

HEME DEGRADATION WITH PARTICIPATION OF THE SUPEROXIDE RADICAL IN THE PRESENCE OF NADH AND LIPOAMIDE DEHYDROGENASE