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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Rhodobacter capsulatus | - |
- |
- |