Crystal structure of guaiacol and phenol bound to a heme peroxidase

Emma J. Murphy, Clive L. Metcalfe, Chukwudi Nnamchi, Peter C E Moody, Emma L. Raven*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)

22 Citations (Scopus)

Abstract

Guaiacol is a universal substrate for all peroxidases, and its use in a simple colorimetric assay has wide applications. However, its exact binding location has never been defined. Here we report the crystal structures of guaiacol bound to cytochrome c peroxidase (CcP). A related structure with phenol bound is also presented. The CcP-guaiacol and CcP-phenol crystal structures show that both guaiacol and phenol bind at sites distinct from the cytochrome c binding site and from the δ-heme edge, which is known to be the binding site for other substrates. Although neither guaiacol nor phenol is seen bound at the δ-heme edge in the crystal structures, inhibition data and mutagenesis strongly suggest that the catalytic binding site for aromatic compounds is the δ-heme edge in CcP. The functional implications of these observations are discussed in terms of our existing understanding of substrate binding in peroxidases [Gumiero A et al. (2010) Arch Biochem Biophys500, 13-20].

Original languageEnglish
Pages (from-to)1632-1639
Number of pages8
JournalFEBS Journal
Volume279
Issue number9
DOIs
Publication statusPublished - 1 May 2012

Keywords

  • cytochrome c peroxidase
  • guaiacol
  • heme
  • peroxidase
  • phenol

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