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Horseradish peroxidase iron-porphyrin site

Rapid Reaction Kinetics Involving the Iron-Porphyrin Site of Horseradish Peroxidase... [Pg.413]

Both oxidizing equivalents of the hydroperoxide are incorporated into compound I, through an oxygen-atom transfer process ". A free radical is generated elsewhere in the molecule on amino acid residue(s) in the case of yeast cytochrome c peroxidase" and at a site strongly coupled to the iron in horseradish peroxidase . (Compound I of yeast cytochrome c peroxidase is called complex ES in earlier literature.) EPR results on horseradish peroxidase are interpreted in terms of a porphyrin rr-cation radical for compound I . Thus, EPR data prove that one oxidizing equivalent obtained from the hydroperoxide is a free radical species"" ... [Pg.656]

See other pages where Horseradish peroxidase iron-porphyrin site is mentioned: [Pg.430]    [Pg.9]    [Pg.92]    [Pg.50]    [Pg.78]    [Pg.86]    [Pg.364]    [Pg.11]    [Pg.171]    [Pg.431]    [Pg.226]    [Pg.241]   
See also in sourсe #XX -- [ Pg.413 ]



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