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  Absolute diffusion measurements of active enzyme solutions by NMR

Günther, J.-P., Majer, G., & Fischer, P. (2019). Absolute diffusion measurements of active enzyme solutions by NMR. The Journal of Chemical Physics, 150(12): 124201, pp. 124201-1-124201-8. doi:10.1063/1.5086427.

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Item Permalink: https://hdl.handle.net/21.11116/0000-000B-28D4-9 Version Permalink: https://hdl.handle.net/21.11116/0000-000E-4CC9-B
Genre: Journal Article

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 Creators:
Günther, Jan-Philipp, Author
Majer, Günter, Author
Fischer, Peer1, 2, Author                 
Affiliations:
1Max Planck Research Group Micro, Nano, and Molecular Systems, Max Planck Institute for Intelligent Systems, Max Planck Society, ou_1497666              
2Institut für Physikalische Chemie, Universität Stuttgart, ou_persistent22              

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 Abstract: The diffusion of enzymes is of fundamental importance for many biochemical processes. Enhanced or directed enzyme diffusion can alter the accessibility of substrates and the organization of enzymes within cells. Several studies based on fluorescence correlation spectroscopy report enhanced diffusion of enzymes upon interaction with their substrate or inhibitor. In this context, major importance is given to the enzyme fructose-bisphosphate aldolase, for which enhanced diffusion has been reported even though the catalysed reaction is endothermic. Additionally, enhanced diffusion of tracer particles surrounding the active aldolase enzymes has been reported. These studies suggest that active enzymes can act as chemical motors that self-propel and give rise to enhanced diffusion. However, fluorescence studies of enzymes can, despite several advantages, suffer from artefacts. Here, we show that the absolute diffusion coefficients of active enzyme solutions can be determined with Pulsed Field Gradient Nuclear Magnetic Resonance (PFG-NMR). The advantage of PFG-NMR is that the motion of the molecule of interest is directly observed in its native state without the need for any labelling. Furthermore, PFG-NMR is model-free and thus yields absolute diffusion constants. Our PFG-NMR experiments of solutions containing active fructose-bisphosphate aldolase from rabbit muscle do not show any diffusion enhancement for the active enzymes, nor the surrounding molecules. Additionally, we do not observe any diffusion enhancement of aldolase in the presence of its inhibitor pyrophosphate.

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Language(s): eng - English
 Dates: 2018-12-202019-02-112019-03-28
 Publication Status: Issued
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1063/1.5086427
URI: https://pubs.aip.org/aip/jcp/article/150/12/124201/595318/Absolute-diffusion-measurements-of-active-enzyme
BibTex Citekey: Guenther2019
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Title: The Journal of Chemical Physics
  Abbreviation : J. Chem. Phys.
Source Genre: Journal
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Publ. Info: Woodbury, N.Y. : American Institute of Physics
Pages: - Volume / Issue: 150 (12) Sequence Number: 124201 Start / End Page: 124201-1 - 124201-8 Identifier: ISSN: 0021-9606
CoNE: https://pure.mpg.de/cone/journals/resource/954922836226