Change in charge of an unvaried heme contact residue does not cause a major change of conformation in cytochrome c.
Change in charge of an unvaried heme contact residue does not cause a major change of conformation in cytochrome c.
复制标题
不变的血红素接触残基的电荷变化不会引起细胞色素 c 构象的重大变化。
DOI：
10.1016/0014-5793(91)80678-v
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发表时间：
1991
期刊：
影响因子：
3.5
通讯作者：
Moore,GR
中科院分区：
文献类型：
--
作者：
Thurgood,AG;Pielak,GJ;Cutler,RL;Davies,AM;Greenwood,C;Mauk,AG;Smith,M;Williamson,DJ;Moore,GR
The structure of the Ala38 variant of yeast iso-1-cytochromec, in which the previously unchanged Arg38 has been replaced, has been characterised by NMR. The NMR data indicate that the structure of the Ala38 variant is very similar to that of the wild type protein. In particular, the heme environment and interactions of the heme macrocycle are shown to be preserved. Analysis of the chemical shift perturbations to the resonances of Ile35 is shown to be consistent with the change in charge at position 38.The only significant area of conformational change detected was at residues 39 and 58, close to the site of modification. Therefore the redox potential change accompanying the modification [1988, Biochemistry 28, 3198–3197] appears to be a direct consequence of the altered side-chain of residue 38 and not a result of secondary conformational changes induced by the modification.
