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RESEARCH PRODUCT

Accessibility of Protein-Bound Chlorophylls Probed by Dynamic Electron Polarization

Daniel M. PalmAlessandro AgostiniDonatella CarboneraHarald Paulsen

subject

Chlorophyll0301 basic medicineNitroxide mediated radical polymerizationFree RadicalsRadicalElectron010402 general chemistry01 natural scienceslaw.inventionElectron Transport03 medical and health scienceslawGeneral Materials SciencePhysical and Theoretical ChemistryPolarization (electrochemistry)Electron paramagnetic resonanceSpectroscopyChemistryElectron Spin Resonance SpectroscopyProteinsChlorophyll; Electron Spin Resonance Spectroscopy; Electron Transport; Free Radicals; Nitrogen Oxides; Protein Binding; Proteins0104 chemical sciences030104 developmental biologyChemical physicsExcited stateNitrogen OxidesProtein BindingMacromolecule

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.

yearjournalcountryeditionlanguage
2018-01-24The Journal of Physical Chemistry Letters
https://doi.org/10.1021/acs.jpclett.7b03428