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Updated: May 29, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
Infrared multiple photon dissociation action spectroscopy and theoretical studies of triethyl phosphate complexes:
B S Fales1, N O Fujamade, J Oomens
1Department of Chemistry, Wayne State University, Detroit, MI, USA.
Abstract:
The gas-phase structures of protonated and sodium cationized complexes of triethyl phosphate, [TEP + H](+) and [TEP + Na](+), are examined via infrared multiple photon dissociation (IRMPD) action spectroscopy using tunable IR radiation generated by a free electron laser, a Fourier transform ion cyclotron resonance mass spectrometer with an electrospray ionization source, and theoretical electronic structure calculations. Measured IRMPD action spectra are compared to linear IR spectra calculated at the B3LYP/6-31 G(d,p) level of theory to identify the structures accessed in the experimental studies. For comparison, theoretical studies of neutral TEP are also performed. Sodium cationization and protonation produce changes in the central phosphate geometry, including an increase in the alkoxy ∠OPO bond angle and shortening of the alkoxy P-O bond. Changes associated with protonation are more pronounced than those produced by sodium cationization.
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