1H-NMR studies of the coordination geometry at the heme iron and the electronic structure of the heme group in cytochrome c-552 from Euglena gracilis.
The 1H-NMR lines of heme c in reduced and oxidized cytochrome c-552 from Euglena gracilis were individually assigned and the coordination geometry of the axial ligands was investigated. The electronic structure of the heme and the chirality of the axially bound methionine were found to be of the same type as in mammalian cytochrome c, but different from cytochrome c-551 from Pseudomonas aeruginosa. These results provide additional support for a previously proposed correlation between the chirality of attachment of the axial methionine and the electronic wave functions in oxidized cytochromes of the c type. Comparison of mammalian cytochrome c, cytochrome c-551 and cytochrome c-552 indicates that the chirality of the axially bound methionine is not linked with the evolutionary increase of the polypeptide chain length.
D000818:Animals; D001665:Binding Sites; D003574:Cytochrome c Group; D005056:Euglena gracilis / Q000032:analysis*; D006418:Heme / Q000032:analysis*; D007501:Iron / Q000032:analysis; D009682:Magnetic Resonance Spectroscopy; D011485:Protein Binding; D011550:Pseudomonas aeruginosa / Q000032:analysis; D013045:Species Specificity
D003574:Cytochrome c Group; C083951:cytochrome c553; D006418:Heme; C022302:cytochrome C-552; D007501:Iron