In summary, we repurposed and evolved a nonheme Fe enzyme 1-aminocyclopropane-1carboxylic acid oxidase (ACCO) to catalyse C(sp 3 )-H fluorination reactions with excellent levels of chemo-and enantiocontrol. Our evolved Fe-dependent enzyme ACCOCHF constitutes the first new-to-nature C-F bond forming biocatalyst, which has long been sought after in biocatalysis, synthetic biology, and bioinorganic chemistry. By exploiting an underutilised radical mechanism for enzymatic C-F bond formation, the current new-to-nature fluorinating enzymes complement the only naturally occurring fluorinase relying on a closed-shell SN2 mechanism for fluorination. Furthermore, this biocatalytic fluorination represents a rare method for catalytic asymmetric C(sp 3 )-H fluorination and the only radical C-H fluorination with excellent enantiocontrol. The utility of our newly evolved nonheme enzymes was further demonstrated in the gram-scale preparation of enantioenriched organofluorides. Together, the evolution of efficient and selective Fe-dependent fluorinating enzymes affords a valuable tool for the biological synthesis of chiral organofluorine compounds via a C-H functionalization logic, thereby setting the stage for the further advancement of fluorine biocatalysis and synthetic biology.