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Classical enzymatic theory revised by including water motions - RESOLV probes real-time changes in water dynamics during enzymatic reactions


Enzymes are macromolecular biological catalysists that lead most of chemical reactions in living organisms. The main focus of enzymology lies on enzymes themselves, whereas the role of water motions in mediating the biological reaction is often left aside owing to the complex molecular behavior. The groups of Martina Havenith (Cluster of Excellence RESOLV – Ruhr explores Solvation) and Irit Sagi (Weizmann Institue of Science, Israel) revised the classical enzymatic steady state theory by including long-lasting protein-water coupled motions into models of functional catalysis. The study has been conducted by integrating X-ray and terahertz based spectroscopies in conjunction with molecular dynamics simulations. The researchers report their finding in the Proceedings of the National Academy of Science (PNAS).

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