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. 1981 Nov;78(11):6854–6857. doi: 10.1073/pnas.78.11.6854

Amino acid sequences of bacterial cytochromes c' and c-556.

R P Ambler, R G Bartsch, M Daniel, M D Kamen, L McLellan, T E Meyer, J Van Beeumen
PMCID: PMC349150  PMID: 6273892

Abstract

The cytochrome c' are electron transport proteins widely distributed in photosynthetic and aerobic bacteria. We report the amino acid sequences of the proteins from 12 different bacterial species, and we show by sequences that the cytochromes c-556 from 2 different bacteria are structurally related to the cytochromes c'. Unlike the mitochondrial cytochromes c, the heme binding site in the cytochromes c' and c-556 is near the COOH terminus. The cytochromes c-556 probably have a methionine sixth heme ligand located near the NH2 terminus, whereas the cytochromes c' may be pentacoordinate. Quantitative comparison of cytochrome c' and c-556 sequences indicates a relatively low 28% average identity.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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