Mechanism of initial reaction of phenylhydrazine with oxyhemoglobin and effect of ring substitutions on the biomolecular rate constant of this reaction.
Mechanism of initial reaction of phenylhydrazine with oxyhemoglobin and effect of ring substitutions on the biomolecular rate constant of this reaction.
复制标题
苯肼与氧合血红蛋白的初始反应机理以及环取代对该反应的生物分子速率常数的影响。
DOI:
10.1021/bi00539a022
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发表时间:
1982
期刊:
影响因子:
2.9
通讯作者:
Matteson,JL
中科院分区:
文献类型:
--
作者:
Itano,HA;Matteson,JL
Harvey A. Itano* and Jeanne L. Matteson abstract: Phenylhydrazine in the presence of oxygen causes the oxidative denaturation of hemoglobin. The initial step in this process is a bimolecular reaction, probably a two-electron transfer from phenylhydrazine to oxyhemoglobin. The product of this reaction is neither methemoglobin nor deoxyhemoglobin. Superoxide dismutase and catalase eliminate side reactions that increase the apparent rate of this reaction as measured spectrophotometrically at577 nm; scavengers for the hydroxyl radical and singlet oxygen do notaffect this rate either in the presence or in theabsence of these enzymes. Halogen atoms. Addition of phenylhydrazine to a solution of oxyhemoglobin results in precipitation of a form of denatured hemoglobin in which the heme moiety has undergoneoxidative changes. When oxidative denaturation takes place in an intact erythrocyte, the resulting intracellular precipitates are known as Heinz bodies, formation of which leads to severe hemolytic anemia and reticulocytosis. Although induction of anemia with phenylhydrazine is the most common method for obtaining reticulocytes for biochemical studies, the chemical mechanism of phenylhydrazine-promoted oxidative denaturation is not known. The severity of arylhydrazine-induced Heinz-body