| Autor: |
Marcolin G; Department of Chemical Sciences, University of Padova, Via Marzolo 1, I-35131 Padova, Italy., Tumbarello F; Department of Chemical Sciences, University of Padova, Via Marzolo 1, I-35131 Padova, Italy., Fresch E; Department of Chemical Sciences, University of Padova, Via Marzolo 1, I-35131 Padova, Italy., Agostini A; Department of Chemical Sciences, University of Padova, Via Marzolo 1, I-35131 Padova, Italy., Büchel C; Institut für Molekulare Biowissenschaften, Goethe Universität Frankfurt, Max-von-Laue-Straβe 9, 60438 Frankfurt, Germany., Carbonera D; Department of Chemical Sciences, University of Padova, Via Marzolo 1, I-35131 Padova, Italy., Collini E; Department of Chemical Sciences, University of Padova, Via Marzolo 1, I-35131 Padova, Italy. |
| Abstrakt: |
Fucoxanthin Chlorophyll Protein (FCP) is a Light Harvesting Complex found in diatoms and brown algae. It is particularly interesting for its efficiency in capturing the blue-green part of the light spectrum due to the presence of specific chromophores (fucoxanthin, chlorophyll a , and chlorophyll c ). Recently, the crystallographic structure of FCP was solved, revealing the 3D arrangement of the pigments in the protein scaffold. While this information is helpful for interpreting the spectroscopic features of FCP, it has also raised new questions about the potential interactions between fucoxanthin and chlorophyll c . These interactions were suggested by their spatial closeness but have never been experimentally observed. To investigate this possible interaction mechanism, in this work, two-dimensional electronic spectroscopy (2DES) has been applied to study the ultrafast relaxation dynamics of FCP. The experiments captured an instantaneous delocalization of the excitation among fucoxanthin and chlorophyll c , suggesting the presence of a non-negligible coupling between the chromophores. |
