Selected MPI CEC publications
Numerous natural and man-designed transformations of fundamental importance to our daily lives are enabled by transition metal molecular catalysts in solution. Spectroscopy overall provides the means to interrogate not only reactants and products, but also the nature of key reactive species responsible for the desired reactivity. The spectroscopic observables are often not clearly mapped to the atomic structural domain as a consequence of intricate quantum mechanical selection rules of light-matter interaction. To close the loop, molecular modeling is essential to provide chemical insights and to propose electronic structural descriptions consistent with experimental data.
In our group, we employ the synthesis-spectroscopy-theory tripod to drive fundamental research on the key characteristics that enable first-row transition metals to perform C-H functionalization.
While enzymes serve as inspiration to design and improve synthetic catalysts, the investigation of molecular models shed light on enzyme’s structure and mechanism. Lytic polysaccharide monooxygenase1 (LPMO) has a solvent-exposed monocopper site able to activate C-H bonds of insoluble polysaccharide substrates, thus breaking them into smaller segments with potential use as renewable feedstock in fermentative processes. The natural oxygen atom source – O2 or H2O2 – is currently debated.2 The mechanism as well as the key reactive intermediate is unknown. The importance of the first coordination sphere relative to distal amino-acid side chains in the second coordination sphere is also of extreme interest to the design of artificial catalytic systems and confined spaces.
1. Vaaje-Kolstad, G.; Westereng, B.; Horn, S.J.; Liu, Z.; Zhai, H.; Sørlie, M.; Eijsink, V.G.; An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides. Science 2010, 330(6001), 219-22.
2. Bissaro, B.; Røhr, Å.K.; Müller, G.; Chylenski, P.; Skaugen, M.; Forsberg, Z.; Horn, S.J.; Vaaje-Kolstad, G.; Eijsink, V.G.H.; Oxidative cleavage of polysaccharides by monocopper enzymes depends on H2O2. Nat Chem Biol. 2017, 13(10):1123-1128.