Engineering the active site of ascorbate peroxidase.
Understanding the catalytic versatility of haem enzymes, and in particular the relationships that exist between different classes of haem-containing proteins and the mechanisms by which the apo-protein structure controls chemical reactivity, presents a major experimental and theoretical challenge. These issues are discussed in the general context of peroxidase and cytochrome P450 chemistry, and specific issues relating to the catalytic chemistry of ascorbate peroxidase are highlighted.
Lloyd Raven
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Department of Chemistry, University of Leicester, University Road, Leicester, LE1 7RH, U.K. emma.raven@le.ac.uk
Celik
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A
Cullis
P M
PM
Sangar
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R
Sutcliffe
M J
MJ
D060387:Ascorbate Peroxidases; D001665:Binding Sites; D003408:Cresols / Q000378:metabolism; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry / Q000378:metabolism; D006418:Heme / Q000378:metabolism; D008958:Models, Molecular; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000737:chemistry* / Q000378:metabolism*; D015202:Protein Engineering; D013379:Substrate Specificity; D013440:Sulfides / Q000378:metabolism
D003408:Cresols; D013440:Sulfides; C032538:4-cresol; D006418:Heme; D003577:Cytochrome P-450 Enzyme System; D010544:Peroxidases; D060387:Ascorbate Peroxidases