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  Direct observation of ultrafast collective motions in CO myoglobin upon ligand dissociation

Barends, T. R., Foucar, L., Ardevol, A., Nass, K., Aquila, A., Botha, S., et al. (2015). Direct observation of ultrafast collective motions in CO myoglobin upon ligand dissociation. Science, 350(6259), 445-450. doi:10.1126/science.aac5492.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-40AC-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-40AD-C
Genre: Journal Article

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 Creators:
Barends, Thomas R.M.1, Author              
Foucar, Lutz2, Author              
Ardevol, Albert3, Author              
Nass, Karol1, Author              
Aquila, Andrew4, Author
Botha, Sabine1, Author              
Doak, R. Bruce1, Author              
Falahati, Konstantin5, Author
Hartmann, Elisabeth2, Author              
Hilpert, Mario2, Author              
Heinz, Marcel3, 5, Author              
Hoffmann, Matthias C.6, Author
Köfinger, Jürgen3, Author              
Koglin, Jason E.6, Author
Kovacsova, Gabriela1, Author              
Liang, Mengning6, Author
Milathianaki, Despina6, Author
Lemke, Henrik T.6, Author
Reinstein, Jochen2, Author              
Roome, Christopher M.2, Author              
Shoeman, Robert L.1, Author              Williams, Garth J.6, AuthorBurghardt, Irene5, AuthorHummer, Gerhard3, Author              Boutet, Sébastien6, AuthorSchlichting, Ilme1, Author               more..
Affiliations:
1Coherent diffractive imaging, Max Planck Institute for Medical Research, Max Planck Society, ou_1497692              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
3Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068292              
4European XFEL GmbH, Albert-Einstein-Ring 19, 22761 Hamburg, Germany, ou_persistent22              
5Institut für Physikalische und Theoretische Chemie, Goethe-Universität, Max-von-Laue-Straße 7, 60438 Frankfurt am Main, Germany, ou_persistent22              
6Linac Coherent Light Source (LCLS), SLAC National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, CA 94025, USA , ou_persistent22              

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 Abstract: The hemoprotein myoglobin is a model system for the study of protein dynamics. We used time-resolved serial femtosecond crystallography at an x-ray free-electron laser to resolve the ultrafast structural changes in the carbonmonoxy myoglobin complex upon photolysis of the Fe-CO bond. Structural changes appear throughout the protein within 500 femtoseconds, with the C, F, and H helices moving away from the heme cofactor and the E and A helices moving toward it. These collective movements are predicted by hybrid quantum mechanics/molecular mechanics simulations. Together with the observed oscillations of residues contacting the heme, our calculations support the prediction that an immediate collective response of the protein occurs upon ligand dissociation, as a result of heme vibrational modes coupling to global modes of the protein.

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Language(s): eng - English
 Dates: 2015-05-122015-08-262015-09-102015-10-23
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1126/science.aac5492
 Degree: -

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Title: Science
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Association for the Advancement of Science
Pages: - Volume / Issue: 350 (6259) Sequence Number: - Start / End Page: 445 - 450 Identifier: ISSN: 0036-8075
CoNE: https://pure.mpg.de/cone/journals/resource/991042748276600_1