Hay, Sam, Pudney, Christopher R., McGrory, Tom A., Pang, Jiayun ORCID: https://orcid.org/0000-0003-0689-8440, Sutcliffe, Michael J. and Scrutton, Nigel S. (2009) Barrier compression enhances an enzymatic hydrogen-transfer reaction. Angewandte Chemie International Edition, 48 (8). pp. 1452-1454. ISSN 1433-7851 (Print), 1521-3773 (Online) (doi:10.1002/anie.200805502)

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Abstract

Putting the squeeze on: Hydrostatic pressure causes a shortening of the charge-transfer bond in the binary complex of morphinone reductase and NADH4 (see diagram). Molecular dynamics simulations suggest that pressure reduces the average reaction barrier width by restricting the conformational space available to the flavin mononucleotide and NADH within the active site. The apparent rate of catalysis increases with pressure.

Item Type:	Article
Uncontrolled Keywords:	enzyme catalysis, hydrogen transfer, molecular dynamics, quantum chemistry, reaction barrier
Subjects:	Q Science > QH Natural history > QH301 Biology
Faculty / School / Research Centre / Research Group:	Faculty of Engineering & Science Faculty of Engineering & Science > School of Science (SCI)
Related URLs:	Publisher Organisation
Last Modified:	21 Oct 2020 22:09
URI:	http://gala.gre.ac.uk/id/eprint/9517

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