C-N and C-S bond formation by cytochrome P450 enzymes

Cytochrome P450 proteins comprise a large family of enzymes that utilize a heme cofactor to perform a diverse array of chemical transformations during secondary metabolite biosynthesis in plants and microorganisms. These en-zymes typically catalyze monooxygenation reactions such as hydroxylation and epoxidation, using O2 as a cosubstrate. However, recent natural product biosynthetic studies revealed that they play crucial roles in morphing the unique architectures of natural products by facilitating atypical carbon-heteroatom bond-forming reactions. In this review, we describe the biosynthetic roles and possible reaction mechanisms of cytochrome P450 enzymes catalyzing unusual carbon-heteroatom bond formation, covering the literature published in the past 5 years.