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外文期刊>The biochemical journal
>Evidence for a conserved binding motif of the dinuclear metal site in mammalian and plant purple acid phosphatases: 1H NMR studies of the di-iron derivative of the Fe(III)Zn(II) enzyme from kidney bean
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Evidence for a conserved binding motif of the dinuclear metal site in mammalian and plant purple acid phosphatases: 1H NMR studies of the di-iron derivative of the Fe(III)Zn(II) enzyme from kidney bean
pThe di-iron core of mammalian purple acid phosphatases has been reproduced in the plant enzyme from kidney bean (iM/isubr/sub 111000) upon insertion of an Fe(II) ion in place of the native zinc(II) in the dinuclear Fe(III)Zn(II) core. The shortening of the electronic relaxation time of the metal centre allows detection of hyperfine-shifted sup1/supH NMR resonances, although severe broadening due to Curie relaxation prevents independent signal assignment. Nevertheless, comparison of the spectral features of the structurally characterized plant enzyme with those of the mammalian species, which were previously extensively assigned, is consistent with a close similarity of the metal-binding sites, also suggested by previous sequence-alignment studies. Some differences appear to be mainly localized at the M(II) site. Spectral comparison was also carried out on the Fe(III)Co(II) derivatives./p
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机译:>通过插入Fe(II),从菜豆( M i> r sub> 111000)的植物酶中复制了哺乳动物紫色酸性磷酸酶的双铁核心。离子代替双核Fe(III)Zn(II)核心中的天然锌(II)。金属中心电子弛豫时间的缩短允许检测到超细位移的 1 sup> H NMR共振,尽管由于居里弛豫导致的严重展宽阻止了独立的信号分配。然而,结构特征化的植物酶的光谱特征与哺乳动物物种的光谱特征的比较,先前被广泛分配,与金属结合位点的紧密相似性一致,这也被先前的序列比对研究所暗示。一些差异似乎主要集中在M(II)站点。还对Fe(III)Co(II)衍生物进行了光谱比较。 p>
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