Bertini I, Briganti F, Luchinat C, Messori L, Monnanni R, Scozzafava A, Vallini G
Department of Chemistry, University of Florence, Italy.
FEBS Lett. 1991 Sep 9;289(2):253-6. doi: 10.1016/0014-5793(91)81082-j.
Oxidized ferredoxin from Clostridium pasteurianum, containing two Fe4S4 clusters, has been investigated using 2D 1H NMR spectroscopy at 600 MHz. 2D NMR experiments allowed complete assignment of the sixteen isotropically shifted signals corresponding to the beta-CH2 protons of the eight metal coordinated cysteines. Geminal connectivities of Cys beta-CH2 protons were identified through magnitude COSY experiments and confirmed through 2D NOESY experiments. A few additional signals could be assigned to the corresponding alpha-CH protons. The importance of 2D experiments to achieve firm assignments of isotropically shifted signals in paramagnetic metalloproteins is stressed.
已使用600兆赫的二维氢核磁共振波谱法对来自巴氏梭菌的含有两个Fe4S4簇的氧化型铁氧化还原蛋白进行了研究。二维核磁共振实验能够完全确定与八个金属配位半胱氨酸的β-CH2质子相对应的十六个各向同性位移信号。通过幅度COSY实验确定了半胱氨酸β-CH2质子的偕偶连接，并通过二维NOESY实验得到了证实。还可以将一些额外的信号归属于相应的α-CH质子。强调了二维实验对于在顺磁性金属蛋白中实现各向同性位移信号的确切归属的重要性。
