Stereochemistry of the porphyrin-protein bond of cytochrome c. Stereochemical comparison of Rhodospirillum rubrum, yeast, and horse heart porphyrins c.
Porphyrins c have been obtained from Rhodospirillum rubrum cytochrome c2, yeast cytochrome c, and horse heart cytochrome c and compared using proton magnetic resonance and circular dichroism. Identity of the spectra establishes that chemically and stereochemically the three porphyrins c are identical. Since the stereochemistry of the porphyrin alpha-thioether linkage is not affected in the conversion to porphyrin c, the stereochemistry at the porphyrin alpha-thioether bonds among the corresponding cytochromes c also must be the same. Differences between the proton magnetic resonance of R. rubrum cytochrome c2 and horse heart cytochrome c which were rationalized by invoking an opposite stereochemistry at these condensation sites (Smith, G. M., and Kamen, M. D. (1974), Proc. Natl. Acad. Sci. U.S.A. 71, 4303) must therefore be attributed to other factors.
D000818:Animals; D001665:Binding Sites; D002942:Circular Dichroism; D003574:Cytochrome c Group / Q000378:metabolism; D006736:Horses; D009682:Magnetic Resonance Spectroscopy; D008280:Magnetics; D009206:Myocardium / Q000201:enzymology*; D011166:Porphyrins; D011485:Protein Binding; D011487:Protein Conformation; D012247:Rhodospirillum rubrum / Q000201:enzymology*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013045:Species Specificity
D003574:Cytochrome c Group; D011166:Porphyrins