Low-temperature spectroscopy of bacteriochlorophyll c aggregates
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Absorption MeSH
- Bacterial Proteins analysis chemistry MeSH
- Bacteriochlorophylls analysis chemistry MeSH
- Fluorescence MeSH
- Oxidation-Reduction MeSH
- Spectrum Analysis methods MeSH
- Temperature MeSH
- Vitamin K 2 chemistry MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- bacteriochlorophyll c MeSH Browser
- Bacterial Proteins MeSH
- Bacteriochlorophylls MeSH
- Vitamin K 2 MeSH
Chlorosomes from green photosynthetic bacteria belong to the most effective light-harvesting antennas found in nature. Quinones incorporated in bacterichlorophyll (BChl) c aggregates inside chlorosomes play an important redox-dependent photo-protection role against oxidative damage of bacterial reaction centers. Artificial BChl c aggregates with and without quinones were prepared. We applied hole-burning spectroscopy and steady-state absorption and emission techniques at 1.9 K and two different redox potentials to investigate the role of quinones and redox potential on BChl c aggregates at low temperatures. We show that quinones quench the excitation energy in a similar manner as at room temperature, yet the quenching process is not as efficient as for chlorosomes. Interestingly, our data suggest that excitation quenching partially proceeds from higher excitonic states competing with ultrafast exciton relaxation. Moreover, we obtained structure-related parameters such as reorganization energies and inhomogeneous broadening of the lowest excited state, providing experimental ground for theoretical studies aiming at designing plausible large-scale model for BChl c aggregates including disorder.
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