A reinvestigation of the covalent structure of Pseudomonas aeruginosa cytochrome c peroxidase.
The amino acid sequence of cytochrome c peroxidase from Pseudomonas aeruginosa has been determined using classical chemical degradation techniques combined with accurate mass analysis of all the generated peptides. The sequence obtained is composed of 346 amino acids and confirms the recently published cDNA-derived sequence except at one position [Ridout et al. (1995) FEBS Lett. 365, 152-154]. Based on this sequence, we propose a new model for the binding of the peroxide and the cytochrome electron donor to CCP which is in essence the reverse of the one proposed by Ellfolk et al.
Samyn
B
B
Department of Biochemistry, University of Gent, Belgium.
Van Craenenbroeck
K
K
De Smet
L
L
Vandenberghe
I
I
Pettigrew
G
G
Van Beeumen
J
J
D000595:Amino Acid Sequence; D003578:Cytochrome-c Peroxidase / Q000737:chemistry* / Q000378:metabolism; D006418:Heme / Q000378:metabolism; D008969:Molecular Sequence Data; D010545:Peroxides / Q000378:metabolism; D011550:Pseudomonas aeruginosa / Q000201:enzymology*
D010545:Peroxides; D006418:Heme; D003578:Cytochrome-c Peroxidase