Life uses very little energy and produces minimal waste when performing chemical reactions. This is why green chemistry looks to life for inspiration: so that it can produce a multitude of industrially interesting molecules more efficiently and at lower cost.

To achieve this, laboratories are seeking to exploit protein catalysts known as metalloenzymes, which can accelerate chemical reactions up to several million times. However, these metalloenzymes are not capable of catalyzing all of the chemical reactions that lead to the industry's products, and they lack stability. This is why researchers have created artificial metalloenzymes by inserting an inorganic metal catalyst into an inactive protein structure. The inorganic part plays the role of the active site of the enzyme, whereas the protein part provides the selectivity of the reaction.

The Irig researchers created several metalloenzymes using a protein responsible for nickel transport in bacteria, to which they anchored various inorganic complexes such as iron, manganese or ruthenium. Next, they made these metalloenzymes solid using a special crystallization technique called "cross linking", which improved the stability of the catalytic site.

Crystalline metalloenzymes obtained this way have made it possible to synthesize models of molecules used in the pharmaceutical industry, such as sulfoxidation products of thioglycolamide derivatives, with an eightfold increase in efficiency even in the presence of very small amounts of catalyst (0.1%). Moreover, these metalloenzymes are capable of multiple catalytic cycles under harsh conditions, considering that the oxidant used for the reaction, sodium hypochlorite, is very aggressive.

The contribution of these new bio-inspired crystalline metalloenzymes is very promising for the development of green chemistry.