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.
School of Biological Sciences, University of Sussex, Brighton, BN1 9QG, UK. a.t.smith@sussex.ac.uk
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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