Kinetic analysis of compound I formation and the catalatic activity of chloroperoxidase

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Abstract
When the only substrate added to a solution of chloroperoxidase [isolated from Caldariomyces fumago] is a hydroperoxide, the reactions are ferric enzyme + ROOH .fwdarw. compound I + ROH and compound I + ROOH .fwdarw. ferric enzyme + O2 + ROH. When H2O2 is used as substrate, the rate constants for the formation and catalatic decomposition of compound I are 2.4 .times. 106 M-1 .cntdot. s-1 and 3.4 .times. 105 M-1 .cntdot. s-1 at pH 4.7; a maximum of 87% of the enzyme apparently converts to compound I in the steady state of the catalatic reaction. With methyl hydroperoxide, formation of compound I has a rate constant of 4.7 .times. 105 M-1 .cntdot. s-1 and its decomposition 2.9 .times. 104 M-1 .cntdot. s-1. When peracetic acid is used, compound I is formed with a rate constant of 3.8 .times. 106 M-1 .cntdot. s-1 and a 100% yield of compound I is obtained.

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