Identifying function-enhancing enzyme variants is a 'holy grail'challenge in protein science
because it will allow researchers to expand the biocatalytic toolbox for late-stage …

Non-heme iron halogenases and hydroxylases activate inert C–H bonds to selectively
catalyze the functionalization of diverse biological products under physiological conditions …

Nonheme iron halogenases are unique enzymes in nature that selectively activate an
aliphatic C–H bond of a substrate to convert it into C–X (X= Cl/Br, but not F/I). It is proposed …

Abstract FeII/α-ketoglutarate (FeII/αKG)-dependent enzymes offer a promising biocatalytic
platform for halogenation chemistry owing to their ability to functionalize unactivated C–H …

Protein engineering holds immense promise in sha** the future of biomedicine and
biotechnology. This Review focuses on our ongoing development of Mutexa, a …

The challenge of activating inert C–H bonds motivates a study of catalysts that draws from
what can be accomplished by natural enzymes and translates these advantageous features …

Biocatalytic C–H activation has the potential to merge enzymatic and synthetic strategies for
bond formation. FeII/αKG-dependent halogenases are particularly distinguished for their …

Deoxypodophyllotoxin contains a core of four fused rings (A to D) with three consecutive
chiral centers, the last being created by the attachment of a peripheral trimethoxyphenyl ring …

Selective halogenation is necessary for a range of fine chemical applications, including the
development of therapeutic drugs. While synthetic processes to achieve C–H halogenation …

Non-heme iron (FeII), α-ketoglutarate (α-KG)-dependent oxygenases are a family of
enzymes that catalyze an array of transformations that cascade forward after the formation of …