意大利佛罗伦萨大学Claudio Luchinat课题组在研究中取得进展。他们提出了从顺磁金属蛋白的磁性特性获得其配位环境的高分辨率信息。 这一研究成果发表在2021年2月17日出版的国际学术期刊《德国应用化学》上。

在这项工作中，研究组表明有可能以其他技术无法到达的分辨率确定蛋白质中顺磁性金属的配位环境。以反磁性类似物的结构为起点，通过将从第一性原理量子化学计算中获得的伪接触位移拟合到实验中来进行几何优化。

据悉，金属蛋白是所有生物蛋白质组的重要组成部分，其特性对于基础科学和生物医学应用都是至关重要的。大量金属蛋白与顺磁金属离子结合，顺磁核磁共振已被广泛应用于其结构表征。然而，紧挨着金属中心的原子核信号往往会因为展宽而超出探测范围。

附：英文原文

Title: A high‐resolution view of the coordination environment in a paramagnetic metalloprotein from its magnetic properties

Author: Enrico Ravera, Lucia Gigli, Elizaveta A. Suturina, Vito Calderone, Marco Fragai, Giacomo Parigi, Claudio Luchinat

Issue&Volume: 2021-02-17

Abstract: Metalloproteins constitute a significant fraction of the proteome of all organisms and their characterization is critical for both basic sciences and biomedical applications. A large portion of metalloproteins bind paramagnetic metal ions, and paramagnetic NMR has been widely used in their structural characterization. However, the signals of nuclei in the immediate vicinity of the metal center are often broadened beyond detection. In this work, we show that it is possible to determine the coordination environment of the paramagnetic metal in the protein at a resolution  inaccessible to other techniques. Taking the structure of a diamagnetic analogue as a starting point, a geometry optimization is carried out by fitting the pseudocontact shifts obtained from first principles Quantum Chemical calculations to the experimental ones.

DOI: 10.1002/anie.202101149

Source: https://onlinelibrary.wiley.com/doi/10.1002/anie.202101149