Projects per year
Abstract
The role of protein dynamics in promoting catalysis is hotly debated. Infrared data from both ultrafast flash photolysis and stopped-flow studies show that not only does there appear to be vibrational coupling between the cofactor and protein in B12-dependent ethanolamine ammonia lyase, but also that there are significant protein motions coupled to the reaction that follows substrate binding (see picture). © 2012 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
Original language | English |
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Pages (from-to) | 9306-9310 |
Number of pages | 4 |
Journal | Angewandte Chemie International Edition |
Volume | 51 |
Issue number | 37 |
DOIs | |
Publication status | Published - 10 Sept 2012 |
Keywords
- enzymes
- infrared spectroscopy
- protein dynamics
- reaction mechanism
- ultrafast spectroscopy
Research Beacons, Institutes and Platforms
- Photon Science Institute
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Dive into the research topics of 'Protein motions are coupled to the reaction chemistry in coenzyme B 12-dependent ethanolamine ammonia lyase'. Together they form a unique fingerprint.Projects
- 1 Finished
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Linking experiment to theory: Quantum entanglement during enzyme catalysis - Dr S Hay fellowship
Hay, S. (PI)
1/09/10 → 31/08/15
Project: Research