Ultrafast Structural Fluctuations of Myoglobin-Bound Thiocyanate and Selenocyanate Ions Measured with Two-Dimensional Infrared Photon Echo Spectroscopy
- Authors
- Maj, Michal; Kwak, Kyungwon; Cho, Minhaeng
- Issue Date
- 16-11월-2015
- Publisher
- WILEY-V C H VERLAG GMBH
- Keywords
- IR spectroscopy; myoglobin; protein dynamics; ultrafast vibrational dynamics; vibrational spectroscopy
- Citation
- CHEMPHYSCHEM, v.16, no.16, pp.3468 - 3476
- Indexed
- SCIE
SCOPUS
- Journal Title
- CHEMPHYSCHEM
- Volume
- 16
- Number
- 16
- Start Page
- 3468
- End Page
- 3476
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/91892
- DOI
- 10.1002/cphc.201500606
- ISSN
- 1439-4235
- 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.
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