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

Barends, Thomas R.M.; Foucar, Lutz; Ardevol, Albert; Nass, Karol; Aquila, Andrew; Botha, Sabine; Doak, R. Bruce; Falahati, Konstantin; Hartmann, Elisabeth; Hilpert, Mario; Heinz, Marcel; Hoffmann, Matthias C.; Köfinger, Jürgen; Koglin, Jason E.; Kovacsova, Gabriela; Liang, Mengning; Milathianaki, Despina; Lemke, Henrik T.; Reinstein, Jochen; Roome, Christopher M.; Shoeman, Robert L.; Williams, Garth J.; Burghardt, Irene; Hummer, Gerhard; Boutet, Sébastien; Schlichting, Ilme

doi:10.1126/science.aac5492

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

MPG-Autoren

/persons/resource/persons92083

Barends, Thomas R.M.
Coherent diffractive imaging, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons92933

Foucar, Lutz
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons194667

Ardevol, Albert
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons117928

Nass, Karol
Coherent diffractive imaging, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons117990

Botha, Sabine
Coherent diffractive imaging, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons117878

Doak, R. Bruce
Coherent diffractive imaging, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons117815

Hartmann, Elisabeth
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons183393

Hilpert, Mario
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons194669

Heinz, Marcel
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;
Institut für Physikalische und Theoretische Chemie, Goethe-Universität, Max-von-Laue-Straße 7, 60438 Frankfurt am Main, Germany;

/persons/resource/persons194635

Köfinger, Jürgen
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons183396

Kovacsova, Gabriela
Coherent diffractive imaging, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons94928

Reinstein, Jochen
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons183399

Roome, Christopher M.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons95345

Shoeman, Robert L.
Coherent diffractive imaging, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons15259

Hummer, Gerhard
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons95189

Schlichting, Ilme
Coherent diffractive imaging, Max Planck Institute for Medical Research, Max Planck Society;

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Zitation

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.

Zitierlink: https://hdl.handle.net/11858/00-001M-0000-002A-40AC-E

Zusammenfassung

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.