Oxidation of hemoglobin and myoglobin by alkyl nitrites inhibition by oxygen.

The reactions of human hemoglobin and sperm whale myoglobin with ethyl nitrite under aerobic conditions have been examined in kinetic detail. Ethyl nitrite converts two equivalents of oxyhemoglobin or oxymyoglobin to their oxidized counterparts with concurrent production of one equivalent each of molecular oxygen, nitrate ion, and ethyl alcohol. Inverse first order kinetic dependence on the concentration of molecular oxygen has been observed and is interpreted by a mechanism in which oxygen dissociation from the oxyhemoprotein occurs prior to rate-limiting oxidation by ethyl nitrite. The rate constant for ethyl nitrite oxidation of hemoglobin from which the fourth oxygen has dissociated is calculated to be 45 times greater than the corresponding rate constant for oxidation of deoxyhemoglobin. This rate enhancement is proposed to be a reflection of the oxidative susceptibility of the R and T conformational states of hemoglobin. Results obtained for the oxidation of myoglobin confirm this interpretation as do kinetic data for hemoglobin and myoglobin oxidations by iron(III) and copper(II) complexes. The effects of organic phosphates on rates for hemoglobin oxidations are interpreted in terms of oxidation inhibition by molecular oxygen.