Abstract
Putting the squeeze on: Hydrostatic pressure causes a shortening of the charge-transfer bond in the binary complex of morphinone reductase and NADH 4 (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. © 2009 Wiley-VCH Verlag GmbH amp; Co. KGaA.
Original language | English |
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Pages (from-to) | 1452-1454 |
Number of pages | 2 |
Journal | Angewandte Chemie - International Edition |
Volume | 48 |
Issue number | 8 |
DOIs | |
Publication status | Published - 9 Feb 2009 |
Keywords
- Enzyme catalysis
- Hydrogen transfer
- Molecular dynamics
- Quantum chemistry
- Reaction barrier