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Haem binding to horse spleen ferritin and its effect on the rate of iron release.

机译:血红素与马脾铁蛋白的结合及其对铁释放速率的影响。

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摘要

Horse spleen ferritin is shown to bind haem to generate a haemoprotein, named herein haemoferritin. A total of 14-16 haem molecules are bound per 24 subunits of ferritin. The molecular mass of the non-haem-iron-free haemoferritin has been determined to be 420 +/- 40 kDa, indicating that haem binding does not lead to dissociation of the 24 subunits that comprise the ferritin molecule. The functional role of the bound haem has been investigated with respect to the release of iron from the non-haem iron core. The bound haem is shown to increase the rate of iron release in a reductive assay system. In the absence of haem the rate of iron release depends on the redox potential of the reductant, but in the presence of haem the rate is largely independent of the reductant and is faster than the rate for the haem-free ferritin. These data haem, but in the presence of haem electron transfer is not rate-limiting.
机译:已显示马脾铁蛋白结合血红素以产生血红蛋白,在此称为血铁蛋白。每24个亚铁蛋白结合总共14-16个血红素分子。已确定非不含血红素铁的血铁蛋白的分子量为420 +/- 40 kDa,这表明血红素结合不会导致组成铁蛋白分子的24个亚基解离。关于从非血红素铁心释放铁的问题,已研究了结合血红素的功能作用。结合血红素在还原测定系统中显示出增加铁释放的速率。在没有血红素的情况下,铁的释放速率取决于还原剂的氧化还原电势,但是在有血红素的情况下,铁的释放速率在很大程度上与还原剂无关,并且比无血红素的铁蛋白的释放速率快。这些数据是血红素,但是在血红素存在的情况下,电子传递不受速率的限制。

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