The incorporation of a synthetic, catalytically competent metallocofactor into a protein
scaffold to generate an artificial metalloenzyme (ArM) has been explored since the late …

Ferritin, a distinctive iron-storage protein, possesses a unique cage-like nanoscale structure
that enables it to encapsulate and deliver a wide range of biomolecules. Recent advances …

Artificial metalloenzymes (ArMs), which combine an abiotic metal cofactor with a protein
scaffold, catalyze various synthetically useful transformations. To complement the natural …

Artificial (transfer) hydrogenases have been developed for organic synthesis, but they rely
on precious metals. Native hydrogenases use Earth‐abundant metals, but these cannot be …

Artificial metalloenzymes, resulting from incorporation of a metal cofactor within a host
protein, have received increasing attention in the last decade. The directed evolution is …

Ferritin, a naturally occuring iron-storage protein, plays an important role in
nanoengineering and biomedical applications. Upon iron removal, apoferritin was shown to …

The streptavidin scaffold was expanded with well-structured naturally occurring motifs.
These chimeric scaffolds were tested as hosts for biotinylated catalysts as artificial …

The intramolecular addition of tosylureas to allenes is highly syn-/anti-diastereoselective
when employing a palladium or rhodium-based catalytic system and affords 1, 3-cyclic …

Diamine ligands I–IV coordinated to an iridium metal complex with the biotin moiety
anchored to the Cp* ring were investigated. This strategy, in contrast to the traditional biotin …

Upregulation of an Artificial Zymogen by Proteolysis - Liu - 2016 - Angewandte Chemie - Wiley
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