Keller R M, Wüthrich K
Biochim Biophys Acta. 1977 Apr 25;491(2):416-22. doi: 10.1016/0005-2795(77)90284-7.
The resonances of the aromatic rings in the 1H NMR spectra at 360 MHz of ferrocytochrome c-552 of Euglena gracilis were investigated by double resonance techniques. The spin systems of the two tryptophan and four of the tyrosine residues could be identified. This analysis of the aromatic region of the 1H NMR spectrum provided evidence that His-14 is bound to the heme iron. It gave also some insight into the molecular dynamics of ferrocytochrome c-552 in that it showed that of the six aromatic rings, four tyrosines were rotating rapidly about the Cbeta-Cgamma bond, while one tyrosine and the single phenylalanine were restricted in their rotational mobilities by their environmnent in the protein.
利用双共振技术研究了纤细裸藻的亚铁细胞色素c - 552在360 MHz下的1H NMR谱中芳香环的共振情况。可以识别出两个色氨酸和四个酪氨酸残基的自旋系统。对1H NMR谱芳香区的这种分析提供了组氨酸-14与血红素铁结合的证据。它还对亚铁细胞色素c - 552的分子动力学有了一些了解，因为它表明在六个芳香环中，四个酪氨酸围绕Cβ - Cγ键快速旋转，而一个酪氨酸和单个苯丙氨酸由于其在蛋白质中的环境而旋转迁移率受到限制。
