A reinvestigation of the covalent structure of Pseudomonas aeruginosa cytochrome c peroxidase

FEBS Letters

Van Beeumen, Jozef²  Van Craenenbroeck, Kathleen²  Samyn, Bart²  Vandenberghe, Isabel²  De Smet, Lina²  Pettigrew, Graham¹ 

[1] Department of Preclinical Veterinary Sciences, Royal (Dick) School of Veterinary Studies, University of Edinburgh, Summerhall, Edinburgh EH9 1QH, UK;Department of Biochemistry, Physiology and Microbiology, Laboratory of Protein Structure and Function, University of Gent, Ledeganckstraat 35, 9000 Gent, Belgium

关键词: Cytochrome c peroxidase;    Pseudomonas aeruginosa;    Mass analysis;    Primary structure;    RPLC;    reversed-phase liquid chromatography;    ESMS;    electrospray mass spectrometry;    MALDI;    matrix-assisted laser desorption mass spectrometry;   

DOI  :  10.1016/0014-5793(95)01326-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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].

【 授权许可】

Unknown