Structural investigation of the cofactor-free chloroperoxidases

Journal of Molecular Biology
B HofmannH Hecht

Abstract

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.

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Citations

Jun 13, 2013·Environmental Science and Pollution Research International·John MumboKarl-Werner Schramm
Feb 2, 2010·Biochemistry·De Lu Tyler YinRomas J Kazlauskas
Jan 19, 2010·Proceedings of the National Academy of Sciences of the United States of America·Roberto A SteinerSusanne Fetzner
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