Radical transfer but not heme distal residues is essential for pH dependence of dye-decolorizing activity of peroxidase from Vibrio cholerae.

Abstract excerpt

Dye-decolorizing peroxidase (DyP) is a heme-containing enzyme that catalyzes the degradation of anthraquinone dyes. A main feature of DyP is the acidic optimal pH for dye-decolorizing activity. In this study, we constructed several mutant DyP enzymes from Vibrio cholerae (VcDyP), with a view to identifying the decisive factor of the low pH preference of DyP. Initially, distal Asp144, a conserved residue, was...

Topics

• Amino Acid Substitution
• Amino Acids
• Anthraquinones
• Binding Sites
• Catalysis
• Catalytic Domain
• Coloring Agents
• Crystallography, X-Ray
• Heme
• Histidine
• Hydrogen Bonding
• Hydrogen-Ion Concentration
• Mutation
• Peroxidase
• Vibrio cholerae