The stereochemistry of peroxidase catalysis

T L Poulos, J Kraut
1980 Journal of Biological Chemistry  
A stereochemical mechanism is proposed for the peroxidase-catalyzed heterolytic cleavage of the RO-OH bond. It is based on the 2.5 A structure of cytochrome c peroxidase, model building experiments, and an extensive body of literature on peroxidase biochemistry. The essential features of this mechanism are acid-base catalysis by an invariant distal histidine (His-52 in cytochrome c peroxidase), charge stabilization by an invariant arginine residue (Arg-48), and stabilization of higher oxidation
more » ... states of the heme iron atom by means of interaction between an invariant proximal histidine (His-174) and a nearby buried glutamine-glutamate pair . The indole ring of Trp-01 on the distal side of the heme ring i s probably the site of radical formation in compound I of cytochrome c peroxidase.
pmid:6251047 fatcat:q4ymj4dtn5d5fc4rvrqsna42y4