Journal article
Oscillatory Enzyme Dynamics Revealed by Two-Dimensional Infrared Spectroscopy
The journal of physical chemistry letters, Vol.7(13), pp.2507-2511
07/07/2016
DOI: 10.1021/acs.jpclett.6b01154
PMCID: PMC4939886
PMID: 27305279
Abstract
Enzymes move on a variety of length and timescales. While much is known about large structural fluctuations which impact binding of the substrates and release of products, little is known about faster motions of enzymes and how these motions may influence enzyme catalyzed reactions. This letter reports frequency fluctuations of azide anion bound to the active site of formate dehydrogenase measured via 2D IR spectroscopy. These measurements reveal an underdamped oscillatory component to the frequency-frequency correlation function when the azide is bound to the NAD + ternary complex. This oscillation disappears when the reduced cofactor is added, indicating that the oscillating contributions most likely come from the charged nicotinamide ring. These oscillatory motions may be relevant to donor-acceptor distance sampling of the catalyzed hydride transfer, and therefore may give future insights into the dynamic behavior involved in enzyme catalysis.
Details
- Title: Subtitle
- Oscillatory Enzyme Dynamics Revealed by Two-Dimensional Infrared Spectroscopy
- Creators
- Philip PaganoQi GuoAmnon KohenChristopher M Cheatum
- Resource Type
- Journal article
- Publication Details
- The journal of physical chemistry letters, Vol.7(13), pp.2507-2511
- DOI
- 10.1021/acs.jpclett.6b01154
- PMID
- 27305279
- PMCID
- PMC4939886
- NLM abbreviation
- J Phys Chem Lett
- ISSN
- 1948-7185
- eISSN
- 1948-7185
- Grant note
- DOI: 10.13039/100000057, name: National Institute of General Medical Sciences, award: R01 GM79368
- Language
- English
- Date published
- 07/07/2016
- Academic Unit
- Core Research Facilities; Chemistry
- Record Identifier
- 9983985890202771
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