Styrene oxidation to styrene oxide in human erythrocytes is catalyzed by oxyhemoglobin
Oxygenated human erythrocytes catalyzed the oxidation of styrene to styrene oxide. This
reaction was inhibited by CO but not by superoxide dismutase, catalase and scavengers of
hydroxyl radicals. In partially deoxygenated erythrocytes styrene oxidation showed a linear
relationship with the molar fraction of oxyhemoglobin. These data indicate that
oxyhemoglobin and not free oxygen radicals are involved in styrene oxidation.
reaction was inhibited by CO but not by superoxide dismutase, catalase and scavengers of
hydroxyl radicals. In partially deoxygenated erythrocytes styrene oxidation showed a linear
relationship with the molar fraction of oxyhemoglobin. These data indicate that
oxyhemoglobin and not free oxygen radicals are involved in styrene oxidation.
Summary
Oxygenated human erythrocytes catalyzed the oxidation of styrene to styrene oxide. This reaction was inhibited by CO but not by superoxide dismutase, catalase and scavengers of hydroxyl radicals. In partially deoxygenated erythrocytes styrene oxidation showed a linear relationship with the molar fraction of oxyhemoglobin. These data indicate that oxyhemoglobin and not free oxygen radicals are involved in styrene oxidation.
Springer
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