Abstract
The complete amino-acid sequence of Pseudomonas cytochrome c-551 consists of 82 amino-acids forming a single peptide chain. The haem is attached to cysteine residues in positions 12 and 15 in the protein sequence, and the only histidine residue of the protein is at position 16. The N-terminal residue of the protein is glutamic-acid, and the C-terminal residue lysine. There is a similarity in charge distribution between the N-terminal portion (residues 1-20) of Pseudomonas cytochrome c-551 and that of horse-heart cytochrome-c. No similarities were noticed between the remainders of the molecules.