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Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/26369

Title: Crystal structure of guaiacol and phenol bound to a heme peroxidase.
Authors: Murphy, EJ
Metcalfe, CL
Nnamchi, C
Moody, PC
Raven, EL
Issue Date: May-2012
Citation: FEBS J, 2012, 279 (9), pp. 1632-1639
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 Biophys 500, 13-20].
DOI Link: 10.1111/j.1742-4658.2011.08425.x
eISSN: 1742-4658
Links: http://hdl.handle.net/2381/26369
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Chemistry

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