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Ultrafast Chemical Exchange Dynamics of Hydrogen Bonds Observed via Isonitrile Infrared Sensors: Implications for Biomolecular Studies

Journal article
Authors Joachim Kübel
G. Lee
Saik Ann Ooi
Sebastian Westenhoff
H. Han
M. Cho
Michal Maj
Published in Journal of Physical Chemistry Letters
Volume 10
Issue 24
Pages 7878-7883
ISSN 1948-7185
Publication year 2019
Published at Department of Chemistry and Molecular Biology
Pages 7878-7883
Language en
Links dx.doi.org/10.1021/acs.jpclett.9b03...
Keywords 2d ir spectroscopy, 2d-ir spectroscopy, jump mechanism, probes, solvatochromism, surface, Chemistry, Science & Technology - Other Topics, Materials Science, Physics
Subject categories Molecular biology, Chemical Sciences

Abstract

Local probes are indispensable to study protein structure and dynamics with site-specificity. The isonitrile functional group is a highly sensitive and H-bonding interaction-specific probe. Isonitriles exhibit large spectral shifts and transition dipole moment changes upon H-bonding while being weakly affected by solvent polarity. These unique properties allow a clear separation of distinct subpopulations of interacting species and an elucidation of their ultrafast dynamics with two-dimensional infrared (2D-IR) spectroscopy. Here, we apply 2D-IR to quantify the picosecond chemical exchange dynamics of solute solvent complexes forming between isonitrile-derivatized alanine and fluorinated ethanol, where the degree of fluorination controls their H-bond-donating ability. We show that the molecules undergo faster exchange in the presence of more acidic H-bond donors, indicating that the exchange process is primarily dependent on the nature of solvent-solvent interactions. We foresee isonitrile as a highly promising probe for studying of H-bonds dynamics in the active site of enzymes.

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