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A reinvestigation of the covalent structure of Pseudomonas aeruginosa cytochrome c peroxidase.
Department of Biochemistry, University of Gent, Belgium.
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.
PMID: 8543038 [PubMed - indexed for MEDLINE]
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Cited by 2 PubMed Central articles
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Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies.
Kim HS, Schell MA, Yu Y, Ulrich RL, Sarria SH, Nierman WC, DeShazer D.
BMC Genomics. 2005 Dec 7; 6:174. Epub 2005 Dec 7.
[BMC Genomics. 2005]
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MacA, a diheme c-type cytochrome involved in Fe(III) reduction by Geobacter sulfurreducens.
Butler JE, Kaufmann F, Coppi MV, Núñez C, Lovley DR.
J Bacteriol. 2004 Jun; 186(12):4042-5.
[J Bacteriol. 2004]