HNO binding in a heme protein: structures, spectroscopic properties, and stabilities.
HNO binding in a heme protein: structures, spectroscopic properties, and stabilities.
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DOI：
10.1021/ja204072j
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发表时间：
2011-09-07
影响因子：
15
通讯作者：
Zhang, Yong
中科院分区：
文献类型：
--
作者：
Yang, Liu;Ling, Yan;Zhang, Yong
HNO可以与许多血红素蛋白相互作用，但原子水平的结构在很大程度上是未知的。在这项工作中，各种结构模型的第一个稳定的HNO血红素蛋白复合物，MbHNO（Mb，肌红蛋白），进行了量子化学计算。这项研究发现了两种新的结构模型，可以很好地再现许多实验光谱特性。它们也是第一个可以解释实验观察到的高稳定性的原子级结构。这两个模型涉及两个远端His构象，如先前报道的MbCNR和MbNO。然而，一个独特的双氢键的HNO结合的特点是没有报道之前在血红素蛋白复合物与其他小分子，如CO，NO，和O2。这些结果将有助于调查HNO结合在其他血红素蛋白。
HNO can interact with numerous heme proteins, but atomic level structures are largely unknown. In this work, various structural models for the first stable HNO heme protein complex, MbHNO (Mb, myoglobin), were examined by quantum chemical calculations. This investigation led to the discovery of two novel structural models that can excellently reproduce numerous experimental spectroscopic properties. They are also the first atomic level structures that can account for the experimentally observed high stabilities. These two models involve two distal His conformations as reported previously for MbCNR and MbNO. However, a unique dual hydrogen bonding feature of the HNO binding was not reported before in heme protein complexes with other small molecules such as CO, NO, and O2. These results shall facilitate investigations of HNO bindings in other heme proteins.
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