Abstract
Summary The optical spectrum of the primary peroxide compound of myeloperoxidase (compound I) is reported. The spectrum, obtained in 1 msec after mixing native ferric myeloperoxidase with excess hydrogen peroxide, exhibits a Soret maximum at 425 nm (c = 52 mM−1 cm−1) and an increase in extinction of the ferric peroxidase at wavelengths higher than 607 nm. The spectrum suggests a structure for compound I of myeloperoxidase similar to those of horseradish peroxidase and catalase. Compound I spontaneously decays to the secondary compound (compound II) in a half time of ⋍ 100 msec. The role of compound I in chloride peroxidation is discussed.
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