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

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Title: Direct observation of ultrafast collective motions in CO myoglobin upon ligand dissociation.
Authors: 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, Mengning Liang, Milathianaki, Despina, Lemke, Henrik T., Reinstein, Jochen, Roome, Christopher M.
Source: Science (pre-March 2025). 10/23/2015, Vol. 350 Issue 1659, p445-450. 6p.
Subjects: Ligands (Biochemistry), Myoglobin, Molecular dynamics, Carbon monoxide, Picosecond pulses, Proteins, Charts, diagrams, etc.
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. [ABSTRACT FROM AUTHOR]
Copyright of Science (pre-March 2025) is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Psychology and Behavioral Sciences Collection
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  Data: Direct observation of ultrafast collective motions in CO myoglobin upon ligand dissociation.
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  Data: <searchLink fieldCode="JN" term="%22Science+%28pre-March+2025%29%22">Science (pre-March 2025)</searchLink>. 10/23/2015, Vol. 350 Issue 1659, p445-450. 6p.
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  Data: <searchLink fieldCode="DE" term="%22Ligands+%28Biochemistry%29%22">Ligands (Biochemistry)</searchLink><br /><searchLink fieldCode="DE" term="%22Myoglobin%22">Myoglobin</searchLink><br /><searchLink fieldCode="DE" term="%22Molecular+dynamics%22">Molecular dynamics</searchLink><br /><searchLink fieldCode="DE" term="%22Carbon+monoxide%22">Carbon monoxide</searchLink><br /><searchLink fieldCode="DE" term="%22Picosecond+pulses%22">Picosecond pulses</searchLink><br /><searchLink fieldCode="DE" term="%22Proteins%22">Proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Charts%2C+diagrams%2C+etc%2E%22">Charts, diagrams, etc.</searchLink>
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  Data: 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. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Science (pre-March 2025) is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1126/science.aac5492
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        Text: English
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      – SubjectFull: Molecular dynamics
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      – SubjectFull: Picosecond pulses
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      – SubjectFull: Charts, diagrams, etc.
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