X-ray fluorescence holography of biological metal sites: Application to myoglobin

X-ray fluorescence holography of biological metal sites: Application to myoglobin
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生物金属位点的 X 射线荧光全息术:在肌红蛋白中的应用

DOI:
10.1016/j.bbrc.2022.10.003
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发表时间:
2022
影响因子:
3.1
通讯作者:
Hayashi Kouichi
Hayashi Kouichi
中科院分区:
生物学4区
文献类型:
--
作者:
Sato-Tomita Ayana;Ang Artoni Kevin R.;Kimura Koji;Marumi Riho;Happo Naohisa;Matsushita Tomohiro;Park Sam-Yong;Shibayama Naoya;Sasaki Yuji C.;Hayashi Kouichi

文献摘要

相似文献

x射线荧光全息(XFH)是一种相对较新的技术,能够提供晶体样品中作为光源的特定原子周围独特的三维结构信息。到目前为止,XFH通常应用于无机材料,如金属和半导体的掺杂剂。在这里,我们研究了使用XFH可视化抹香鲸肌红蛋白(Mb)中金属活性位点的可能性,Mb是一种单体氧储存血红素蛋白。我们证明了从碳氧肌红蛋白(MbCO)晶体的全息图数据重建的原子图像与晶体结构是中等一致的,这也是本研究在近原子分辨率下通过x射线晶体学和模拟结果确定的。这些结果为XFH应用于生物分子中金属位点的局部原子和电子结构成像开辟了新的途径。
X-ray fluorescence holography (XFH) is a relatively new technique capable of providing unique three-dimensional structural information around specific atoms that act as a light source in crystalline samples. So far, XFH has typically been applied to inorganic materials such as dopants in metals and semiconductors. Here, we investigate the possibility of using XFH to visualize the metal active site in sperm whale myoglobin (Mb), a monomeric oxygen storage heme protein. We demonstrate that the atomic images reconstructed from the hologram data of crystals of carbonmonoxy myoglobin (MbCO) are moderately consistent with the crystal structure, which is also determined in this study by X-ray crystallography in the near-atomic resolution, as well as simulation results. These results open up a new avenue for the application of XFH to local atomic and electronic structure imaging of metal-sites in biomolecules.