Ultrafast Structural Fluctuations of Myoglobin-Bound Thiocyanate and Selenocyanate Ions Measured with Two-Dimensional Infrared Photon Echo Spectroscopy

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Abstract

Structural dynamics within the distal cavity of myoglobin protein is investigated using 2D-IR and IR pump-probe spectroscopy of the N≡C stretch modes of heme-bound thiocyanate and selenocyanate ions. Although myoglobin-bound thiocyanate group shows a doublet in its IR absorption spectrum, no cross peaks originating from chemical exchange between the two components are observed in the time-resolved 2D IR spectra within the experimental time window. Frequency-frequency correlation functions of the two studied anionic ligands are obtained by means of a few different analysis approaches; these functions were then used to elucidate the differences in structural fluctuation around ligand, ligand-protein interactions, and the degree of structural heterogeneity within the hydrophobic pocket of these myoglobin complexes.

Original languageEnglish
Pages (from-to)3468-3476
Number of pages9
JournalChemPhysChem
Volume16
Issue number16
DOIs
Publication statusPublished - 2015 Nov 16

Keywords

  • IR spectroscopy
  • myoglobin
  • protein dynamics
  • ultrafast vibrational dynamics
  • vibrational spectroscopy

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Atomic and Molecular Physics, and Optics

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