NMR characterization of surface interactions in the cytochrome b5-cytochrome c complex.
NMR characterization of surface interactions in the cytochrome b5-cytochrome c complex.
复制标题
细胞色素 b5-细胞色素 c 复合物表面相互作用的 NMR 表征。
DOI：
10.1126/science.2154849
复制
发表时间：
1990
期刊：
影响因子：
--
通讯作者：
Moore,GR
中科院分区：
文献类型：
--
作者：
Burch,AM;Rigby,SE;Funk,WD;MacGillivray,RT;Mauk,MR;Mauk,AG;Moore,GR
The complex formed in solution by native and chemically modified cytochrome c with cytochrome b5has been studied by1H and13C nuclear magnetic resonance spectroscopy (NMR). Contrary to predictions of recent theoretical analysis,1H NMR spectroscopy indicates that there is no major movement of cytochrome c residue Phe82on binding to cytochrome b5. The greater resolution provided by13C NMR spectroscopy permits detection of small perturbations in the environments of cytochrome c residues Ile75and Ile85on binding with cytochrome b5, a result that is in agreement with earlier model-building experiments. As individual cytochrome c lysyl residues are resolved in the1H NMR spectrum ofN-acetimidylated cytochrome c, the interaction of this modified protein with cytochrome b5has been studied to evaluate the number of cytochrome c lysyl residues involved in binding to cytochrome b5. The results of this experiment indicate that at least six lysyl residues are involved, two more than predicted by static model building, which indicates that cytochrome c and cytochrome b5form two or more structurally similar 1:1 complexes in solution.
