Structural homology of cytochromes c.
Cytochromes c from many eukaryotic and diverse prokaryotic organisms have been investigated and compared using high-resolution nuclear magnetic resonance spectroscopy. Resonances have been assigned to a large number of specific groups, mostly in the immediate environment of the heme. This information, together with sequence data, has allowed a comparison of the heme environment and protein conformation for these cytochromes. All mitochondrial cytochromes c are found to be very similar to the cytochromes c2 from Rhodospirillaceae. In the smaller bacterial cytochromes, Pseudomonas aeruginosa cytochrome c551 and Euglena gracilis cytochrome c552, the orientation of groups near the heme is very similar, but the folding of the polypeptide chain is different. The heme environment of these two proteins is similar to that of the larger bacterial and mitochondrial cytochromes. Two low-potential cytochromes, Desulfovibrio vulgaris cytochrome c553 and cytochrome c554 from a halotolerant micrococcus have heme environments which are not very similar to those of the other proteins reported here.
D000596:Amino Acids; D000818:Animals; D001419:Bacteria / Q000201:enzymology; D003574:Cytochrome c Group / Q000235:genetics; D005399:Fishes; D006418:Heme; D006736:Horses; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D008928:Mitochondria / Q000201:enzymology; D011487:Protein Conformation; D013045:Species Specificity
D000596:Amino Acids; D003574:Cytochrome c Group; D008024:Ligands; D006418:Heme