This work was funded by the UK Biotechnology and Biological Sciences Research Council (BBSRC). N.S.S. is a BBSRC Professorial Research Fellow.
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Communication
Barrier Compression Enhances an Enzymatic Hydrogen-Transfer Reaction†
Article first published online: 14 JAN 2009
DOI: 10.1002/anie.200805502
Copyright © 2009 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Hay, S., Pudney, Christopher R., McGrory, Tom A., Pang, J., Sutcliffe, Michael J. and Scrutton, Nigel S. (2009), Barrier Compression Enhances an Enzymatic Hydrogen-Transfer Reaction. Angew. Chem. Int. Ed., 48: 1452–1454. doi: 10.1002/anie.200805502
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Publication History
- Issue published online: 30 JAN 2009
- Article first published online: 14 JAN 2009
- Manuscript Received: 11 NOV 2008
Funded by
- UK Biotechnology and Biological Sciences Research Council (BBSRC)
Keywords:
- enzyme catalysis;
- hydrogen transfer;
- molecular dynamics;
- quantum chemistry;
- reaction barrier
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.