6533b831fe1ef96bd1299050
RESEARCH PRODUCT
How the Protein Environment Can Tune the Energy, the Coupling, and the Ultrafast Dynamics of Interacting Chlorophylls: The Example of the Water-Soluble Chlorophyll Protein
Elena MeneghinAlessandro AgostiniAlessandro AgostiniElisa FreschHarald PaulsenDonatella CarboneraElisabetta Collinisubject
ChlorophyllModels MolecularLetterChemistryChlorophyll ALight-Harvesting Protein ComplexesTemperatureWater02 engineering and technology010402 general chemistry021001 nanoscience & nanotechnology01 natural sciences0104 chemical sciencesCoupling (physics)chemistry.chemical_compoundProtein environmentWater solubleChemical physicsChlorophyllThermodynamicsMoleculeGeneral Materials SciencePhysical and Theoretical Chemistry0210 nano-technologyUltrashort pulsedescription
The interplay between active molecules and the protein environment in light-harvesting complexes tunes the photophysics and the dynamical properties of pigment–protein complexes in a subtle way, which is not fully understood. Here we characterized the photophysics and the ultrafast dynamics of four variants of the water-soluble chlorophyll protein (WSCP) as an ideal model system to study the behavior of strongly interacting chlorophylls. We found that when coordinated by the WSCP protein, the presence of the formyl group in chlorophyll b replacing the methyl group in chlorophyll a strongly affects the exciton energy and the dynamics of the system, opening up the possibility of tuning the photophysics and the transport properties of multichromophores by engineering specific interactions with the surroundings.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2020-01-17 |