The role of several residues located between the cluster and heme in the catalytic reaction is probed in mutagenesis experiments. The edge-to-edge straight-line distance between the cluster and heme is approx. FMN and the cluster are positioned closely, which facilitates efficient electron shuttling. The continuous polypeptide chain comprises three functional domains, which align well with the direction of electrons traveling from FMN to the heme through the cluster. Here, we present the crystal structure of full-length CYP116B46, a self-sufficient P450. Self-sufficient cytochrome P450 enzymes contain the redox partners in a single polypeptide chain.
Cytochrome P450 monooxygenases are versatile heme-thiolate enzymes that catalyze a wide range of reactions.
