Veitch N C, Concar D W, Williams R J, Whitford D
Inorganic Chemistry Laboratory, University of Oxford, England.
FEBS Lett. 1988 Sep 26;238(1):49-55. doi: 10.1016/0014-5793(88)80223-0.
Two-dimensional 1H NMR spectroscopy is used to examine the structure and mobility of cytochrome b5 in solution. The assignment of many residues and the interpretation of nuclear Overhauser effects (NOEs) in both redox states allow definition of secondary structural elements. Comparison with X-ray diffraction data shows that differences between crystal and solution structures are small. The dynamics of the protein are examined and the protein is shown to be more mobile than cytochrome c. The relationship of the structure and dynamics to the electron transfer function of cytochrome b5 is discussed.
二维¹H核磁共振光谱用于研究溶液中细胞色素b5的结构和流动性。对两种氧化还原状态下许多残基的归属以及核Overhauser效应（NOE）的解释使得能够定义二级结构元件。与X射线衍射数据的比较表明，晶体结构和溶液结构之间的差异很小。对蛋白质的动力学进行了研究，结果表明该蛋白质比细胞色素c具有更高的流动性。讨论了细胞色素b5的结构和动力学与电子传递功能之间的关系。
