Asymmetry in 13C-13C COSY spectra provides information on ligand geometry in paramagnetic proteins

被引:17
作者
Bertini, I
Jiménez, B
Piccioli, M
Poggi, L
机构
[1] Univ Florence, Magnet Resonance Ctr, I-50019 Florence, Italy
[2] Ecole Normale Super, Dept Chem, F-75005 Paris, France
关键词
D O I
10.1021/ja051058m
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The relative intensity of Cα-C- cross-peaks in homonuclear 13C COSY spectra depends on the relaxation properties of Cα and C- spins, which, in the proximity of a paramagnetic center, are related to the metal-to-carbon distance. Their quantitative analysis has lead, for the cerium-substituted dicalcium protein, calbindin D9k, to the straightforward identification of peaks arising from metal-coordinating groups. The monodentate or bidentate metal binding mode of carboxylates was identified directly via NMR. Copyright © 2005 American Chemical Society.
引用
收藏
页码:12216 / 12217
页数:2
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