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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 oxidationpmid:6251047 fatcat:q4ymj4dtn5d5fc4rvrqsna42y4