Title : Hydroxyl-radical production in physiological reactions. A novel function of peroxidase.

Pub. Date : 1999 Mar

PMID : 10103001






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 We provide evidence that to mediate this reaction, the ferric form of horseradish peroxidase must be converted by O2.- into the perferryl form (Compound III), in which the haem iron can assume the ferrous state. Iron peroxidase Glycine max
2 The .OH-producing activity of horseradish peroxidase can be inhibited by inactivators of haem iron or by various O2.- and .OH scavengers. Iron peroxidase Glycine max
3 On an equimolar Fe basis, horseradish peroxidase is 1-2 orders of magnitude more active than Fe-EDTA, an inorganic catalyst of the Haber-Weiss reaction. Iron peroxidase Glycine max