Abstract
Cytochrome c 553 is an electron donor to P700 in the photosynthetic electron transfer chain of cyanobacteria and eukaryotic algae. We have purified this cytochrome from the cyanobacterium Microcystis aeruginosa and determined its amino acid sequence. When the amino acid sequence of this protein is compared to sequences of cytochromes c 553 from other organisms, one sees that the evolution of net charge is more pronounced than the evolution of overall structure, further documenting a pronounced shift in the isoelectric point of this protein during the evolution of cyanobacteria. Cyanobacteria and algae also contain cytochrome c 550 ( M r 15,500) which is quite different from cytochrome c 553 ( M r 10,500). When the amino acid sequence of cytochrome c 553 is compared to that of cytochrome c 550, two regions of similar sequence are recognized.
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