The two c-type cytochromes of Rhodospirillum molischianum (Dus, K., Flatmark, T., deKlerk, H., and Kamen, M. D. (1970), Biochemistry 9,1984) strikingly resemble cytochrome c of eukaryotic organisms with regard to p7, absorption spectra (at 25°as well as at -190°), and circular dichroism spectra in the Soret and visible wavelength regions. In this respect they differ from previously studied c-type cytochromes (cytochromes c2) of nonsulfur purple photosynthetic bacteria. Although these findings suggest that the chemical nature of the linkages of the hemes to the respective apoproteins may be very similar in the c-type cytochromes of R. molischianum to that in eukaryotic cytochrome c, they should not be taken as evidence for similarity in protein structure surrounding these heme groups. Thus, the oxida-