Feb 25, 1976

Inhibition by superoxide dismutase of methemoglobin formation from oxyhemoglobin

The Journal of Biological Chemistry
R E LynchG E Cartwright

Abstract

The formation of methemoglobin from oxyhemoglobin in a solution containing photoreduced riboflavin and oxygen was inhibited by superoxide dismutase. The rate of the reaction was pH-dependent in the range of 6.8 to 7.8, increasing as the pH was reduced. Inhibition by superoxide dismutase was enhanced as the EDTA concentration increased and was dependent on enzymatic activity. Under conditions in which superoxide dismutase inhibition was incomplete, catalase inhibited the reaction but mannitol had no effect. The data support the mediation of methemoglobin formation by superoxide. The hypothesis is offered that superoxide anion reduced the heme-bound oxygen in oxygemoglobin by one electron, permitting the subsequent dissociation of ferrihemoglobin and peroxide. The ability of superoxide dismutase to inhibit the formation of methemoglobin may represent one of its functions in the mature erythrocyte.

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Mentioned in this Paper

Methemoglobin
Mature Erythrocytes
SOD2
Oxyhemoglobin Measurement
Riboflavin
Methemoglobin Measurement
Edetic Acid, Sodium Salt
Mannitol
Eryhem
Protein Conformation

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