| Cytochrome b562 | |
| Cartoons view of Cytochrome b562, a 4-helix bundle. N-terminus is colored blue, C-terminus is red.
The topology is the same as myohemerythrin.
Cytochrome b562 transfers electrons by using a heme group. The heme binding site is found between the helices. The Fe of the heme is ligated additionally by two amino acids: His 102 and Met 7.
The heme is tightly packed between the N-terminus and the C-terminus.
It is too large to fit within the bundle, and so it must present its polar edge toward the solvent (water).
Lederer, F., Glatigny, A., Bethge, P. H., Bellamy, H. D., Mathews, F. S.: Improvement of the 2.5 Angstroms Resolution Model of Cytochrome B562 by Redetermining the Primary Structure and Using Molecular Graphics J.Mol.Biol. 148 pp. 427 (1981) (PubMed) 256b(PDB) |