Spectral analysis of Fe(III)-complex reduction by hemoglobin: Possible mechanisms of interaction

John P. Harrington, Rodgers L. Hicks
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引用次数: 8

Abstract

  • 1.

    1. Hemoglobin is capable of electron transfer to Fe(III)-complexes of ATP, EDTA, NTA, and citrate leading to formation of reduced Fe(II) and its concurrent release from these chelating compounds as evident in the formation of a Fe(II)-Tris 2,2' bipyridine complex.

  • 2.

    2. Multi-component analysis of kinetic spectra in the visible region (700–500 nm) has permitted a determination of the effect of various chelating molecules bound to Fe(III), pH, the effects of ionic strength, temperature, and the molecular nature of the Fe(III)-complex on reaction rates.

  • 3.

    3. We have examined and compared the reactivities of normal adult hemoglobin A (α2 β2) to reduce these Fe(III)-complexes and suggest possible mechanism(s) for the electron transfer process.

血红蛋白还原铁(III)络合物的光谱分析:可能的相互作用机制
1.1. 血红蛋白能够将电子转移到铁(III)- ATP、EDTA、NTA和柠檬酸盐的络合物上,导致铁(II)的还原形成,并从这些螯合化合物中同时释放铁(II),这在铁(II)-Tris 2,2'联吡啶络合物的形成中是显而易见的。在可见光区(700-500 nm)进行多组分动力学光谱分析,可以确定各种螯合分子与Fe(III)结合的影响、pH、离子强度、温度和Fe(III)-络合物的分子性质对反应速率的影响。我们检查并比较了正常成人血红蛋白A (α2 β2)还原这些Fe(III)-复合物的反应性,并提出了电子转移过程的可能机制。
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