Ultrafast myoglobin structural dynamics observed with an X-ray free-electron laser

Matteo Levantino, Giorgio Schirò, Henrik Till Lemke, Grazia Cottone, James Michael Glownia, Diling Zhu, Mathieu Chollet, Hyotcherl Ihee, Antonio Cupane and Marco Cammarata ()
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Matteo Levantino: University of Palermo
Giorgio Schirò: CNRS, Université Grenoble Alpes, CEA—Institut de Biologie Structurale
Henrik Till Lemke: LCLS, SLAC National Accelerator Laboratory
Grazia Cottone: University of Palermo
James Michael Glownia: LCLS, SLAC National Accelerator Laboratory
Diling Zhu: LCLS, SLAC National Accelerator Laboratory
Mathieu Chollet: LCLS, SLAC National Accelerator Laboratory
Hyotcherl Ihee: Center for Nanomaterials and Chemical Reactions, Institute for Basic Science (IBS)
Antonio Cupane: University of Palermo
Marco Cammarata: UMR UR1-CNRS 6251, University of Rennes 1

Nature Communications, 2015, vol. 6, issue 1, 1-6

Abstract: Abstract Light absorption can trigger biologically relevant protein conformational changes. The light-induced structural rearrangement at the level of a photoexcited chromophore is known to occur in the femtosecond timescale and is expected to propagate through the protein as a quake-like intramolecular motion. Here we report direct experimental evidence of such ‘proteinquake’ observed in myoglobin through femtosecond X-ray solution scattering measurements performed at the Linac Coherent Light Source X-ray free-electron laser. An ultrafast increase of myoglobin radius of gyration occurs within 1 picosecond and is followed by a delayed protein expansion. As the system approaches equilibrium it undergoes damped oscillations with a ~3.6-picosecond time period. Our results unambiguously show how initially localized chemical changes can propagate at the level of the global protein conformation in the picosecond timescale.

Date: 2015
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DOI: 10.1038/ncomms7772

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