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Literature summary for 1.11.1.5 extracted from

  • De Smet, L.; Savvides, S.N.; Van Horen, E.; Pettigrew, G.; Van Beeumen, J.J.
    Structural and mutagenesis studies on the cytochrome c peroxidase from Rhodobacter capsulatus provide new insights into structure-function relationships of bacterial di-heme peroxidases (2006), J. Biol. Chem., 281, 4371-4379.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
fully oxidized form, reveals that a segment of 10 amino acids near the peroxide binding site is disordered in all four molecules of the asymmetric unit of the crystal. Flexibility in this part of the molecular scaffold correlates with the levels of activity seen in cytochrome c peroxidases characterized so far Rhodobacter capsulatus

Protein Variants

Protein Variants Comment Organism
E117H no enzymatic activity Rhodobacter capsulatus
E117K no enzymatic activity Rhodobacter capsulatus
E117L no enzymatic activity Rhodobacter capsulatus
H74M no enzymatic activity, reduced redox potential. The introduced methionine does not ligate the N-terminal heme Rhodobacter capsulatus
M118H no enzymatic activity Rhodobacter capsulatus
M118L 7.3% of wild-type activity Rhodobacter capsulatus
M278H no enzymatic activity, reduced redox potential. Mutant contains two low-potential hemes Rhodobacter capsulatus
Q107L no enzymatic activity Rhodobacter capsulatus
W97A no enzymatic activity. W97 is the mediator of intramolecular electron transfer of the enzyme Rhodobacter capsulatus
W97F no enzymatic activity. W97 is the mediator of intramolecular electron transfer of the enzyme Rhodobacter capsulatus

Organism

Organism UniProt Comment Textmining
Rhodobacter capsulatus
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