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首页> 外文期刊>The Journal of Chemical Physics >Influence of mutations at the proximal histidine position on the Fe-O-2 bond in hemoglobin from density functional theory
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Influence of mutations at the proximal histidine position on the Fe-O-2 bond in hemoglobin from density functional theory

机译：基于密度泛函理论的组氨酸近端突变对血红蛋白中Fe-O-2键的影响

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摘要

Four mutated hemoglobin (Hb) variants and wild type hemoglobin as a reference have been investigated using density functional theory methods focusing on oxygen binding. Dispersion-corrected B3LYP functional is used and found to provide reliable oxygen binding energies. It also correctly reproduces the spin distribution of both bound and free heme groups as well as provides correct geometries at their close vicinity. Mutations in hemoglobin are not only an intrigued biological problem and it is also highly important to understand their effects from a clinical point of view. This study clearly shows how even small structural differences close to the heme group can have a significant effect in reducing the oxygen binding of mutated hemoglobins and consequently affecting the health condition of the patient suffering from the mutations. All of the studied mutated Hb variants did exhibit much weaker binding of molecular oxygen compared to the wild type of hemoglobin. (C) 2016 AIP Publishing LLC.
机译：已经使用集中于氧结合的密度泛函理论方法研究了四个突变的血红蛋白（Hb）变体和野生型血红蛋白作为参考。使用经分散校正的B3LYP官能团可提供可靠的氧结合能。它还可以正确复制结合的和自由的血红素基团的自旋分布，并在它们的近邻处提供正确的几何形状。血红蛋白的突变不仅是一个有趣的生物学问题，而且从临床角度了解其作用也非常重要。这项研究清楚地表明，即使接近血红素组的微小结构差异也可以在减少突变的血红蛋白的氧结合并因此影响遭受突变的患者的健康状况方面发挥显著作用。与野生型血红蛋白相比，所有研究的突变的Hb变异体均表现出弱得多的分子氧结合。 （C）2016 AIP出版有限责任公司。

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