Prof. dr. Maarten Egmond
Quo vadis, Enzymology?
A recent article in Nature (27 May 2019) highlights new opportunities to expand the catalytic machinery of enzymes:
Only a few types of natural amino-acid residue are used directly by enzymes to catalyse reactions. The incorporation of an unnatural residue into an enzyme shows how the catalytic repertoire of enzymes can be enlarged.
In TheScientist (June 1st 2019) Catherine Offord highlighs interesting examples of biological systems where quantum effects may play a role:
"From the remarkable speed of enzyme-catalyzed reactions to the workings of the human brain, numerous biological puzzles are now being explored for evidence of quantum effects".
Already by the mid 1980's Judith Klinman suggested that C-H activation in lipoxygenase catalysis may involve quantum tunneling. Quoting from a recent article (JACS 2017 139 (51): 18409–18427) :
"....This Perspective highlights recent experimental data for two members of distinct, yet iconic C-H activation enzyme classes, lipoxygenases and prokaryotic alcohol dehydrogenases. The data necessitate a reformulation of the dominant textbook definition of biological catalysis. A multidimensional model emerges that incorporates a range of protein motions that can be parsed into a combination of global stochastic conformational thermal fluctuations and local donor- acceptor distance sampling. These motions are needed to achieve a high degree of precision with regard to internuclear distances, geometries, and charges within the active site. The available model also suggests a physical framework for understanding the empirical enthalpic barrier in enzyme-catalyzed processes. We conclude by addressing the often conflicting interface between computational and experimental chemists, emphasizing the need for computation to predict experimental results in advance of their measurement"