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Binding Modes of Aromatic Ligands to Mammalian Heme Peroxidases with Associated Functional Implications: CRYSTAL STRUCTURES OF LACTOPEROXIDASE COMPLEXES WITH ACETYLSALICYLIC ACID, SALICYLHYDROXAMIC ACID, AND BENZYLHYDROXAMIC ACID
The binding and structural studies of bovine lactoperoxidase with three aromatic ligands, acetylsalicylic acid (ASA), salicylhydoxamic acid (SHA), and benzylhydroxamic acid (BHA) show that all the three compounds bind to lactoperoxidase at the substrate binding site on the distal heme side. The bind...
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| Autores principales: | , , , , , , , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
American Society for Biochemistry and Molecular Biology
2009
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2740456/ https://ncbi.nlm.nih.gov/pubmed/19465478 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M109.010280 |
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