Protein chemistry fascinates synthetic chemists, in particular because of the extraordinary speed and selectivity of enzymatic reactions. This is particularly true of molecular oxygen activation, catalyzed by metallo-enzymes, mono-oxygenases or di-oxygenases. This process is of prime importance in the living world, since it enables oxygen from the air to be used in desired, controlled oxidation reactions. Today, a bio-inspired approach to this chemical catalysis consists of partially mimicking the structure of an enzyme's active site in order to reproduce its activity, which nevertheless remains modest due to low selectivity [1].
To get close to the enzyme, we first need to understand its intimate mechanism. This is the subject of this seminar, which presents a new concept for studying the mechanism of chemical metal catalysts, combining protein crystallography and bioinorganic catalysis. In this way, it becomes possible to visually define the various stages of an aromatic hydroxylation reaction using an iron complex, highlighting the role of the metal [2]. This approach has led to the development of new artificial oxygenases capable of enantioselective reactions. These hybrid systems illustrate a new approach to catalysis in the context of green chemistry.
