Accessibility of Protein-Bound Chlorophylls Probed by Dynamic Electron Polarization

Accessibility of Protein-Bound Chlorophylls Probed by Dynamic Electron Polarization

The possibility to probe the accessibility of sites of proteins represents an important point to explore their interactions with specific substrates in solution. The dynamic electron polarization of nitroxide radicals induced by excited triplet states of organic molecules is a phenomenon that is kno...

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Veröffentlicht in:The journal of physical chemistry letters 2018-02, Vol.9 (3), p.672-676
Hauptverfasser: Agostini, Alessandro, Palm, Daniel M, Paulsen, Harald, Carbonera, Donatella
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container_title The journal of physical chemistry letters
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creator Agostini, Alessandro
Palm, Daniel M
Paulsen, Harald
Carbonera, Donatella
description The possibility to probe the accessibility of sites of proteins represents an important point to explore their interactions with specific substrates in solution. The dynamic electron polarization of nitroxide radicals induced by excited triplet states of organic molecules is a phenomenon that is known to occur in aqueous solutions. The interaction within the radical–triplet pair causes a net emissive dynamic electron polarization of the nitroxide radical, that can be detected by means of time-resolved electron paramagnetic resonance (TR-EPR) spectroscopy. We have exploited this effect to prove the accessibility of chlorophylls bound to a protein, namely, the water-soluble chlorophyll protein WSCP. The results have important implications for topological studies in macromolecules.
doi_str_mv 10.1021/acs.jpclett.7b03428
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title Accessibility of Protein-Bound Chlorophylls Probed by Dynamic Electron Polarization
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