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

De novo enzyme design has sought to introduce active sites and substrate-binding pockets
that are predicted to catalyse a reaction of interest into geometrically compatible native …

Many efforts are being made in the design and engineering of metalloenzymes with catalytic
properties fulfilling the needs of practical applications. Progress in this field has recently …

Primordial sequence signatures in modern proteins imply ancestral origins tracing back to
simple peptides. Although short peptides seldom adopt unique folds, metal ions might have …

Artificial metalloenzymes result from anchoring an organometallic catalyst within an
evolvable protein scaffold. Thanks to its dimer of dimers quaternary structure, streptavidin …

We have shown that de novo designed peptides self‐assemble in the presence of copper to
create supramolecular assemblies capable of carrying out the oxidation of dimethoxyphenol …

There are 20 proteinogenic amino acids and a limited number of cofactors naturally
available to build enzymes. Genetic codon expansion enables us to incorporate more than …

Metalloproteins are crucial for life. The mutual relationship between metal ions and proteins
makes metalloproteins able to accomplish key processes in biological systems, often very …

The selective hydroxylation of C–H bonds is of great interest to the synthetic community.
Both homogeneous catalysts and enzymes offer complementary means to tackle this …

Limited bonding valence, usually accompanied by well-defined directional interactions and
selective bonding mechanisms, is nowadays considered among the key ingredients to …