Substrate binding and catalysis in heme peroxidases.
Peroxidase-catalysed reactions are being analysed at an increasingly advanced level of structural and mechanistic sophistication. A significant development in this respect has been the long-anticipated solution of crystal structures for several plant peroxidases and a fungal peroxidase complexed to benzhydroxamic acid. New insights into peroxide binding and catalysis have been obtained through site-directed mutagenesis, a technique also crucial to recent progress in understanding the diversity of substrate interaction sites associated with peroxidases from different sources.
Smith
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School of Biological Sciences, University of Sussex, Brighton, BN1 9QG, UK. a.t.smith@sussex.ac.uk
Veitch
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D001665:Binding Sites / Q000502:physiology; D002384:Catalysis; D018360:Crystallography, X-Ray; D005656:Fungal Proteins / Q000737:chemistry; D006420:Hemeproteins / Q000737:chemistry*; D007700:Kinetics; D008958:Models, Molecular; D010544:Peroxidases / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry; D011485:Protein Binding / Q000502:physiology; D017433:Protein Structure, Secondary
D005656:Fungal Proteins; D006420:Hemeproteins; D010940:Plant Proteins; D010544:Peroxidases