Structure-mechanism relationships in hemoproteins. Oxygenations catalyzed by chloroperoxidase and horseradish peroxidase.

Chloroperoxidase and H2O2 oxidize styrene to styrene oxide and phenylacetaldehyde but not benzaldehyde. The epoxide oxygen is shown by studies with H2(18)O2 to derive quantitatively from the peroxide. The epoxidation of trans-[1-2H]styrene by chloroperoxidase proceeds without detectable loss of stereochemistry, as does the epoxidation of styrene by rat liver cytochrome P-450, although much more phenylacetaldehyde is produced by chloroperoxidase than cytochrome P-450. Chloroperoxidase and cytochrome P-450 thus oxidize styrene by closely related oxygen-transfer mechanisms. Horseradish peroxidase does not oxidize styrene but does oxidize 2,4,6-trimethylphenol to 2,6-dimethyl-4-hydroxymethylphenol. The new hydroxyl group is partially labeled in incubations with H2(18)O but not H2(18)O2. The hydroxyl group thus appears to be introduced by addition of oxygen to the benzylic radical and water to the quinone methide intermediate but not by a cytochrome P-450-like oxene transfer mechanism. The results support the thesis that substrates primarily or exclusively react with the heme edge of horseradish peroxidase but are able to react with the ferryl oxygen of chloroperoxidase.