H-1 NMR study of 2-methylimidazole binding to cytochrome c: a comprehensive investigation of the role of the methyl substituent on the ligand bindingaffinity and heme electronic structure in imidazole-cytochrome c complexes
Y. Yao et al., H-1 NMR study of 2-methylimidazole binding to cytochrome c: a comprehensive investigation of the role of the methyl substituent on the ligand bindingaffinity and heme electronic structure in imidazole-cytochrome c complexes, J CHEM S DA, (12), 2001, pp. 1841-1845
Citations number
30
Categorie Soggetti
Inorganic & Nuclear Chemistry
Journal title
JOURNAL OF THE CHEMICAL SOCIETY-DALTON TRANSACTIONS
The binding of 2-methylimidazole (2mim) to horse heart cytochrome c (hh cyt
c) has been studied by NMR spectroscopy. Some proton resonances were assig
ned and the kinetic and thermodynamic parameters for the binding were prese
nted. Based on its unique hyperfine shift pattern and the anomalous tempera
ture dependence of the heme methyl resonances, the heme electronic structur
e was discussed and the orientation of the bound 2mim was estimated. With t
hese data, a comprehensive comparison of imidazole (Him), 4-methylimidazole
(4mim) and 2mim bound cyt c complexes was made on the ligand binding affin
ity and the heme electronic structure. Different properties in these ligand
-cyt c complexes provide a useful lesson for the study of protein-small mol
ecular interactions.