Non-Heme Iron Enzyme Mimicry Through Confinement

Biological enzymes have evolved over billions of years to mediate kinetically challenging transformations under mild conditions and with excellent selectivities. Inspired by nature, our group works at the interface of bioinorganic chemistry and materials science toward the precise engineering of void spaces that can kinetically stabilize high-valent, bio-inspired complexes. This talk will focus principally on the chemistry of bio-inspired high-valent iron-oxo and iron-nitrosyl species that have been kinetically stabilized through confinement within a rigid macrocycle. The unique thermal stabilities of these species enable novel investigations of their photochemical behaviors both in solution and in the solid state. Most notably, photocrystallographic studies have illuminated novel C-C cleavage reactions mediated by “oxyl”-type excited states of a confined high-spin iron(IV)-oxo. Mechanistic studies of reactions arising from direct photoexcitation of this complex will be discussed. At the end of the talk, I will briefly highlight our work using dynamic porous solids for separation science and energy storage.

Speaker: Brandon Barnett, University of Rochester