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A reinvestigation of the covalent structure of Pseudomonas aeruginosa cytochrome c peroxidase
Author(s) -
Samyn Bart,
Van Craenenbroeck Kathleen,
De Smet Lina,
Vandenberghe Isabel,
Pettigrew Graham,
Van Beeumen Jozef
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01326-1
Subject(s) - cytochrome c peroxidase , peroxidase , chemistry , peptide sequence , cytochrome c , pseudomonas aeruginosa , sequence (biology) , cytochrome , stereochemistry , amino acid , biochemistry , complementary dna , peroxide , enzyme , biology , organic chemistry , bacteria , genetics , gene , mitochondrion
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. [Biochim. Biophys. Acta 1080 (1991) 175–178].