Abstract
The amino acid sequence of cytochrome c' from the purple photosynthetic bacterium Rhodospirillum rubrum S1 has been determined and is consistent with homology to cytochrome c' from the nonphotosynthetic bacterium Alcaligenes sp. NCIB 11015. There is 29% identity in the chosen alignment of these two proteins. R. rubrum cytochrome c' is composed of a single peptide chain of 126 amino acid residues with a single heme covalently bound near the COOH terminus. There is no sequence similarity to mitochondrial cytochrome c, except at the heme binding site.
Highlights
The amino acid sequence of cytochrome c’ from the purple photosynthetic bacterium Rhodospirillum rubrum Sl has been determined and is consistent with homology to cytochrome c’ from the nonphotosynthetic bacterium Alcaligenes sp
The proposed amino acid sequence of the protein is shown in Fig. 1, along with peptide overlaps
In the restricted area of the heme binding region, there is stronger similarity between Alcaligenes sp. and Chromatium vinosum [3] cytochrome c’ than either shows to the R. rubrum protein
Summary
The amino acid sequence of cytochrome c’ from the purple photosynthetic bacterium Rhodospirillum rubrum Sl has been determined and is consistent with homology to cytochrome c’ from the nonphotosynthetic bacterium Alcaligenes sp. R. rubrum cytochrome c’ is composed of a single peptide chain of 126 amino acid residues with a single heme covalently bound near the COOH terminus. The proposed amino acid sequence of the protein is shown, along with peptide overlaps.3
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