Enzymatic assembly of carbon-carbon bonds via iron-catalysed sp³ C-H functionalization.

ABSTRACT: Although abundant in organic molecules, carbon-hydrogen (C-H) bonds are typically considered unreactive and unavailable for chemical manipulation. Recent advances in C-H functionalization technology have begun to transform this logic, while emphasizing the importance of and challenges associated with selective alkylation at a sp³ carbon^1,2. Here we describe iron-based catalysts for the enantio-, regio- and chemoselective intermolecular alkylation of sp³ C-H bonds through carbene C-H insertion. The catalysts, derived from a cytochrome P450 enzyme in which the native cysteine axial ligand has been substituted for serine (cytochrome P411), are fully genetically encoded and produced in bacteria, where they can be tuned by directed evolution for activity and sel

SUBMITTER: Zhang RK 

PROVIDER: S-EPMC6440214 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature