Help Privacy Policy Disclaimer
  Advanced SearchBrowse




Journal Article

Coherent infrared emission from myoglobin crystals: An electric field measurement


Schlichting,  Ilme
Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available

Groot, M.-L., Vos, M. H., Schlichting, I., van Mourik, F., Joffre, M., Lambry, J.-C., et al. (2002). Coherent infrared emission from myoglobin crystals: An electric field measurement. Proceedings of the National Academy of Sciences of the United States of America, 99(3): 1, pp. 1323-1328. Retrieved from http://dx.doi.org/10.1073/pnas.251662698.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0014-0EE9-F
We introduce coherent infrared emission interferometry as a X(2) vibrational spectroscopy technique and apply it to studying the initial dynamics upon photoactivation of myoglobin (Mb). By impulsive excitation (using 11-fs pulses) of a Mb crystal, vibrations that couple to the optical excitation are set in motion coherently. Because of the order in the crystal lattice the coherent oscillations of the different proteins in the crystal that are associated with charge motions give rise to a macroscopic burst of directional multi-teraHertz radiation. This radiation can be detected in a phase-sensitive way by heterodyning with a broad-band reference field. In this way both amplitude and phase of the different vibrations can be obtained. We detected radiation in the 1,000-1,500 cm(-1) frequency region, which contains modes sensitive to the structure of the heme macrocycle, as well as peripheral protein modes. Both in carbonmonoxy-Mb and aquomet-Mb we observed emission from six modes, which were assigned to heme vibrations. The phase factors of the modes contributing to the protein electric field show a remarkable consistency, taking on values that indicate that the dipoles are created "emitting" at t = 0, as one would expect for impulsively activated modes. T e few deviations from this behavior in Mb-CO we propose are the result of these modes being sensitive to the photodissociation process and severely disrupted by it.