Engineering and Analysis of a Self-Sufficient Biosynthetic Cytochrome P450 PikC Fused to the RhFRED Reductase Domain

摘要

Cytochrome P450 enzymes (P450s) are highly attractive bio-catalysts due to their ability to catalyze a variety of regio- and stereospecific oxidation reactions of complex organic compounds. These reactions occur under mild conditions by taking advantage of the two-electron activated dioxygen that is often challenging in organic synthesis. To activate molecular oxygen, redox partners are required to sequentially transfer two reducing equivalents from NAD(P)H to P450. Classically, there are two major redox partner systems, including an FAD containing reductase with a small iron-sulfur (Fe_2S_2) redoxin for most bacterial and mitochondrial P450s (class I) and a single FAD/FMN containing flavoprotein for eukaryotic microsomal P450s (class Ⅱ). The inherent requirement of cytochome P450s for separate protein partner(s) significantly limits their application in biotechnology.