Designing and synthesis of DPAs ligands to induce structural modification of Riboflavin

One of the most fascinating aspects of enzymes is the way these biological catalysts have been designed in order to be able to carry out highly selective reactions under mild conditions. Controlled modification and artificial tuning of Nature’s legacy, using molecular biology technices together with new chemical methods in the field o f bioorganic syntheses, led chemists to investigate access to modified proteins, going as far as designing artificial enzymes.

Ferrous complexes with aromatic α-substituted tris(2-pyridylmethyl)amine ligands: effect of the substituents and biomimetic reactivity

Biomimetic oxidations at active sites of iron proteins involve peroxides, especially hydrogen peroxide which is a strong and very convenient reagent since it is inexpensive and does not release any toxic by-products. In many cases however, mother Nature uses molecular dioxygen to carry out major oxidation reactions in particularly attractive conditions. The biomimetic interest of iron complexes in the tris(2-pyridylmethyl)amine series TPA is no longer to demonstrate. We prepared various α-substituted TPA-based ligands with the idea to modulate the electronic properties at the metal centre. We then checked the reactivity of a one example of complexes towards molecular dioxygen.