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Updated: Aug 11, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
Direct observation of substrate distortion by triosephosphate isomerase using Fourier transform infrared spectroscopy
Abstract:
The infrared spectrum of dihydroxyacetone phosphate bound to triosephosphate isomerase has been measured. There are two carbonyl bands corresponding to the bound substrate, with an intensity ratio of about 3:1. Relative to the carbonyl absorption of dihydroxyacetone phosphate in free solution, the major band is shifted by 19 cm-1 to 1713 cm-1, providing direct evidence of enzyme-induced distortion of the substrate. This strain is probably attributable to an enzymic electrophile that polarizes the carbonyl group of the substrate and thereby promotes catalysis.
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