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Updated: Mar 22, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
Overall biochemical changes in bacteria photosensitized with cationic porphyrins monitored by infrared spectroscopy
Eliana Alves1, Catarina Moreirinha2, Maria Af Faustino2
1Department of Biology & CESAM, University of Aveiro, Campus Universitário de Santiago, 3810-193 Aveiro, Portugal.
Background:
Photodynamic inactivation of micro-organisms is a promising nonantibiotic multitarget approach to treat localized and superficial infections through oxidative stress. Herein, the changes occurring on major cellular components of Escherichia coli and Staphylococcus warneri, induced by photosensitization with cationic porphyrins (Tri-Py(+)-Me-PF and Tetra-Py(+)-Me) and white light, were monitored by infrared spectroscopy.
Results:
In E. coli, most of the changes occurred on proteins and lipids, suggesting a key effect on lipopolysaccharides in the first irradiation times. In S. warneri, proteins were the major molecular targets of oxidative damage but phospholipids and polysaccharides were also affected.
Conclusion:
Infrared spectroscopy is a very interesting tool to monitor biochemical changes induced by photosensitization in bacteria and also to infer on its mechanism of action.
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