Chloroperoxidase (CPO), the most versatile heme protein, has a hybrid active site pocket that shares structural features with peroxidases and cytochrome P450s. We find that the versatility of CPO's catalytic activity is enhanced by the apoenzyme's ability to efficiently utilize its peroxidase-P450 hybrid construction and take on structurally different peroxidase and P450 faces. We present studies of the apoenzyme's effects on the catalytic cycle of CPO-catalyzed epoxidation of cis-�-methylstyrene.

Versatility of chloroperoxidase catalytic function: Apoenzyme tunes reactivity of the active center

245th National Meeting (2013)

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