Structural investigation of the cofactor-free chloroperoxidases

J Mol Biol. 1998 Jun 19;279(4):889-900. doi: 10.1006/jmbi.1998.1802.


The structures of cofactor-free haloperoxidases from Streptomyces aureofaciens, Streptomyces lividans, and Pseudomonas fluorescens have been determined at resolutions between 1.9 A and 1.5 A. The structures of two enzymes complexed with benzoate or propionate identify the binding site for the organic acids which are required for the haloperoxidase activity. Based on these complexes and on the structure of an inactive variant, a reaction mechanism is proposed for the halogenation reaction with peroxoacid and hypohalous acid as reaction intermediates. Comparison of the structures suggests that a specific halide binding site is absent in the enzymes but that hydrophobic organic compounds may fit into the active site pocket for halogenation at preferential sites.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Chloride Peroxidase / chemistry*
  • Chloride Peroxidase / genetics
  • Chloride Peroxidase / metabolism
  • Crystallography, X-Ray
  • Molecular Sequence Data
  • Protein Conformation
  • Pseudomonas / enzymology*
  • Sequence Alignment
  • Sequence Analysis
  • Streptomyces / enzymology*
  • Structure-Activity Relationship


  • Bacterial Proteins
  • Chloride Peroxidase