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

Barends, T. R. M., 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-0000-0028-7387-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-3129-D
Genre: Journal Article

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Barends, Thomas R. M.1, Author              
Foucar, Lutz1, Author              
Ardevol, Albert, Author
Nass, Karol1, Author              
Aquila, Andrew, Author
Botha, Sabine1, Author              
Doak, R. Bruce1, Author              
Falahati, Konstantin, Author
Hartmann, Elisabeth1, Author              
Hilpert, Mario1, Author              
Heinz, Marcel, Author
Hoffmann, Matthias C., Author
Köfinger, Jürgen, Author
Koglin, Jason E., Author
Kovácsová, Gabriela1, Author              
Liang, Mengning, Author
Milathianaki, Despina, Author
Lemke, Henrik, Author
Reinstein, Jochen1, Author              
Roome, Christopher M.1, Author              
Shoeman, Robert L.1, Author              Williams, Garth J., AuthorBurghardt, Irene, AuthorHummer, Gerhard, AuthorBoutet, Sébastien, AuthorSchlichting, Ilme1, Author               more..
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Abstract: The hemoprotein myoglobin is a model system to study protein dynamics. We used time-resolved serial femtosecond crystallography at an x-ray free-electron laser to resolve the ultrafast structural changes taking place in the carbonmonoxy myoglobin complex upon photolysis of the Fe-CO bond. Structural changes appear throughout the protein within 500 fs with the C-, F- and H-helices moving away from the heme and the E- and A-helices moving toward it. These collective movements are predicted by quantum mechanics/molecular mechanics simulations. Together with the observed oscillations of residues contacting the heme, the calculations support predictions that an immediate collective response of the protein takes place upon ligand dissociation due to coupling of vibrational modes of the heme 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: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 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