The solution structure of bovine cytochrome b 5 mutant (E44A/E48A/E56A/D60A) has been obtained from 1H NMR spectra measured at 600 MHz. The final RMSD values with respect to the average structure are (0.056±0.009) nm and (0.105±0.010) nm for backbone and all heavy atoms, respectively. The solution structure, when compared with the X ray structure of wild type, has no significant changes in the whole folding and secondary structure. Small changes are restricted to local conformation near mutated sites. [WT5HZ]
The solution structure of the imidazole adduct of oxidized horse heart cytochrome c(Im cyt c) has been determined through 2D NMR spectroscopy. The 35 conformers of the family show the RMSD values to the average structure of 0.063±0.007 nm for the backbone and 0.107±0.007 nm for all heavy atoms, respectively. The secondary structure elements and the overall folding of the present structure are substantially similar to those of the solution structure of native protein. However, the replacement of the axial ligand Met 80 with the exogenous imidazole ligand induces significant conformation changes in both backbone and side chains of the residues locating in the distal axial ligand regions. The electron delocalization on the heme moiety and the magnetic susceptibility tensor are consistent with these structural features.
吴义兵陆军姚勇白志平唐雯霞朱德熙BANCI LuciaBERTINI IvanoLIU GaohuaREDDIG Tim
