Dynamic motion and rearranged molecular shape of heme in myoglobin: structural and functional consequences.

Dynamic motion and rearranged molecular shape of heme in myoglobin: structural and functional consequences.
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肌红蛋白中血红素的动态运动和重新排列的分子形状:结构和功能后果。

DOI:
10.3390/molecules18033168
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发表时间:
2013-03-11
期刊:
Molecules (Basel, Switzerland)
影响因子:
--
通讯作者:
Neya S
Neya S
中科院分区:
其他
文献类型:
--
作者:
Neya S

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肌红蛋白,一种简单的氧结合蛋白,与各种类型的合成血红素重组操纵血红素-珠蛋白的相互作用。从顺磁NMR分析,小血红素被发现快速旋转的铁-组氨酸键。这是蛋白质波动的一个新的典型例子。动态NMR分析表明,在室温下,一个小血红素的360°旋转速率为1,400 s−1。X射线衍射分析表明,尽管血红素-珠蛋白相互作用被破坏,但含有最小血红素的珠蛋白的三级结构与天然蛋白的三级结构非常相似。氧结合的功能分析表明,松散的血红素-珠蛋白接触不显着影响氧结合。另外,四吡咯阵列的重排和卟啉环的非平面形变也对肌红蛋白的功能性质有重要影响。这些结果表明,调节肌红蛋白功能的基本因素隐藏在辅基的分子形状下,而不是在非键合的血红素-珠蛋白接触中。
Myoglobin, a simple oxygen binding protein, was reconstituted with various types of synthetic hemes to manipulate the heme-globin interactions. From the paramagnetic NMR analysis, small heme was found to rotate rapidly about the iron-histidine bond upon. This is a novel and typical example for the fluctuation of protein. The dynamic NMR analysis indicated that the 360° rotational rate of a small heme was 1,400 s−1 at room temperature. The X-ray analyses revealed that the tertiary structure of globin containing the smallest heme was closely similar to that of native protein despite extensive destruction of the specific heme-globin interactions. The functional analyses of O2 binding showed that the loose heme-globin contacts do not significantly affect the oxygen binding. On the other hand, the rearrangement of tetrapyrrole array and the non-planar deformation in porphyrin ring significantly affect the functional properties of myoglobin. These results, taken together, indicate that the essential factors to regulate the myoglobin function are hidden under the molecular shape of prosthetic group rather than in the nonbonded heme-globin contacts.
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