On the evolutionary relationship of the 4-alpha-helical heme proteins. The comparison of cytochrome b562 and cytochrome c'.
The atomic models of the cytochrome b562 and cytochrome c' monomers have been compared. When the respective heme groups are superimposed, the four alpha-helices of each nearly coincide. Four aromatic side chains, including the heme ligands, and a methionine occur in spatially equivalent positions in contact with the heme groups. This structural evidence suggests that the two cytochrome families may have diverged from a common molecular ancestor.
D005075:Biological Evolution; D003573:Cytochrome b Group; D003574:Cytochrome c Group; D003580:Cytochromes; D004926:Escherichia coli; D029968:Escherichia coli Proteins; D006420:Hemeproteins; D008958:Models, Molecular; D008970:Molecular Weight; D011487:Protein Conformation; D012246:Rhodospirillum
D003573:Cytochrome b Group; D003574:Cytochrome c Group; D003580:Cytochromes; D029968:Escherichia coli Proteins; D006420:Hemeproteins; C017850:cytochrome b562, E coli