Abstract
C type cytochromes are a very valuable and long preserved invention in the history of life. The distinguishing characteristic of these molecules is a heme prosthetic group attached to a protein by two covalent thioether bonds. The attachment site in the protein is recognized by its signature amino acid sequence -Cys-X-X-Cys-His-. With the completion of the nucleotide sequence of the genome of Synechocystis PCC 6803 by the Kazusa Institute (Internet address http://www. Kazusa. or. jp), one can recognize this binding site in at least five open reading frames and four of these are identified with gene product proteins that have been isolated and partially characterized. These four are cytochrome f, cytochrome c6, cytochrome M (all of these are easily reduced by ascorbate, so are high potential cytochromes) and low potential cytochrome c549 (reduced by dithionite).
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