Crystal structure of guaiacol and phenol bound to a heme peroxidase.
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 phen...
| Main Authors: | , , , , |
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| Format: | Journal article |
| Language: | English |
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2012
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| _version_ | 1826283708870557696 |
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| author | Murphy, E Metcalfe, C Nnamchi, C Moody, P Raven, E |
| author_facet | Murphy, E Metcalfe, C Nnamchi, C Moody, P Raven, E |
| author_sort | Murphy, E |
| collection | OXFORD |
| description | 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]. |
| first_indexed | 2024-03-07T01:02:58Z |
| format | Journal article |
| id | oxford-uuid:8a586db2-6135-401d-9bfa-5dea11a0d7fd |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T01:02:58Z |
| publishDate | 2012 |
| record_format | dspace |
| spelling | oxford-uuid:8a586db2-6135-401d-9bfa-5dea11a0d7fd2022-03-26T22:30:55ZCrystal structure of guaiacol and phenol bound to a heme peroxidase.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:8a586db2-6135-401d-9bfa-5dea11a0d7fdEnglishSymplectic Elements at Oxford2012Murphy, EMetcalfe, CNnamchi, CMoody, PRaven, EGuaiacol 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]. |
| spellingShingle | Murphy, E Metcalfe, C Nnamchi, C Moody, P Raven, E Crystal structure of guaiacol and phenol bound to a heme peroxidase. |
| title | Crystal structure of guaiacol and phenol bound to a heme peroxidase. |
| title_full | Crystal structure of guaiacol and phenol bound to a heme peroxidase. |
| title_fullStr | Crystal structure of guaiacol and phenol bound to a heme peroxidase. |
| title_full_unstemmed | Crystal structure of guaiacol and phenol bound to a heme peroxidase. |
| title_short | Crystal structure of guaiacol and phenol bound to a heme peroxidase. |
| title_sort | crystal structure of guaiacol and phenol bound to a heme peroxidase |
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