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

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

in Animals / Carbon Monoxide - chemistry / Crystallography / Crystallography, X-Ray / Dynamical systems / Dynamics / Femtosecond / Free electron lasers / Helices / Heme - chemistry / Horses / Iron - chemistry / Lasers / Ligands / Mathematical models / Molecular Dynamics Simulation / Molecular structure / Motion / Myoglobin / Myoglobin - chemistry / Myoglobins / Photolysis / Protein Structure, Secondary / Proteins / Quantum Mechanics

2015

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

2015

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

2015

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Journal Article

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

Falahati, Konstantin,

Kovacsova, Gabriela,

Milathianaki, Despina,

Burghardt, Irene,

Reinstein, Jochen,

Foucar, Lutz,

Doak, R. Bruce,

Botha, Sabine,

Hoffmann, Matthias C.,

Shoeman, Robert L.,

Schlichting, Ilme,

Roome, Christopher M.,

Liang, Mengning,

Ardevol, Albert,

Koglin, Jason E.,

Hartmann, Elisabeth,

Köfinger, Jürgen,

Aquila, Andrew,

Heinz, Marcel,

Barends, Thomas R. M.,

Nass, Karol,

Williams, Garth J.,

Hummer, Gerhard,

Boutet, Sébastien,

Lemke, Henrik T.,

Hilpert, Mario

2015

Overview

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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Publisher

American Association for the Advancement of Science,The American Association for the Advancement of Science

Subject

Animals

/ Carbon Monoxide - chemistry

/ Crystallography

/ Crystallography, X-Ray

/ Dynamical systems

/ Dynamics

/ Femtosecond