IRON-57 AND H-2 NUCLEAR MAGNETIC RESONANCE--NEW TOOLS FOR BIOMEDICAL RESEARCH

我们正在开发铁-57和氘核磁共振(核磁共振)作为一种 用于生物医学科学的实验方法。 许多生命所必需的分子是由含铁的物质构成的 中央核心。其中包括血红蛋白、铁还蛋白和 细胞色素。到目前为止，还没有物理化学方法允许直接 这些蛋白质的中心金属环境的研究。铁-57核磁共振， 即铁核磁共振信号的直接检测，正被开发用于 那就是目的。 早些时候，我们报告了铁-57核磁共振研究的结果 某些铁的特征弛豫时间和化学位移 化合物。这些数据提供了有关化学位移范围的信息。 铁与氮配位，取代基对铁-57化学的影响 铁-57的位移和松弛机制，从而为 进一步开发Fe-57核磁共振所需的参数。最近， 首次在一种名为碳单氧肌球蛋白的蛋白质中观察到57Fe核磁共振 与57Fe弛豫时间的测定和 化学位移各向异性。 我们现在已经扩展了这个项目，以包括对依赖于 铁卟啉的H-2核磁共振。这项工作证实了地球的局部定向 铁的现场卟啉和允许测定磁性 各向异性。

We are developing iron-57 and deuterium Magnetic Resonance (NMR) as an experimental method for use in the Biomedical Sciences. Numerous molecules essential to life are constructed about iron-containing central cores. Among these are hemoglobin, ferridoxin and the cytochromes. To date, no physical chemical methods have allowed direct study of the central metal enviroment of these proteins. Iron-57 NMR, i.e., the direct detection of the iron NMR signal, is being developed for that purpose. Earlier, we reported results of an iron-57 NMR investigation of characteristic relaxation times and chemical shifts of some iron compounds. The data furnished information on the chemical shift range of iron coordinated to nitrogen, substituent effects on iron-57 chemical shifts, and relaxation mechanisms for iron-57, and thus provide the basic parameters needed for further development of iron-57 NMR. Most recently, the first observation of 57Fe NMR in a protein, carbonmonoxymyoglobin, was published together with a determination of 57Fe relaxation times and chemical shift anisotropy. We have now expanded this project to include a study of the field dependent H-2 NMR of iron porphyrins. The work confirms the partial orientation of iron porphyrins in the field and allows the determination of magnetic anisotropies.