Eguchi L A, Saltman P
J Biol Chem. 1984 Dec 10;259(23):14337-8.
The ability of hemoglobin (myoglobin) to reduce directly low-molecular-weight complexes of Fe(III) to form methemoglobin (metmyoglobin) and the Fe(II)-tris(2,2'-bipyridine) complex under aerobic conditions is described. The reduction is not mediated by superoxide, O-.2, as shown by increased rates under anaerobic conditions and lack of inhibition by superoxide dismutase. The chemical nature of the Fe(III) complex presented influences the rate of reduction; one of the most effective chelating agents of cellular origin is Fe(III) X ATP. This mechanism may be of fundamental importance in the mobilization and utilization of iron in biological systems.
描述了血红蛋白（肌红蛋白）在有氧条件下直接将Fe(III)的低分子量复合物还原以形成高铁血红蛋白（高铁肌红蛋白）和Fe(II)-三（2,2'-联吡啶）复合物的能力。如在厌氧条件下速率增加以及超氧化物歧化酶无抑制作用所示，该还原反应不是由超氧阴离子O₂⁻介导的。所呈现的Fe(III)复合物的化学性质会影响还原速率；细胞来源的最有效的螯合剂之一是Fe(III)·ATP。这种机制在生物系统中铁的动员和利用中可能具有根本重要性。
