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.
Asymmetry in 13C-13C COSY spectra provides information on ligand geometry in paramagnetic proteins / I.Bertini; B.Jiménez; M.Piccioli; L.Poggi. - In: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY. - ISSN 0002-7863. - STAMPA. - 127:(2005), pp. 12216-12217. [10.1021/ja051058m]
Asymmetry in 13C-13C COSY spectra provides information on ligand geometry in paramagnetic proteins
BERTINI, IVANO;PICCIOLI, MARIO;
2005
Abstract
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.
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