scholarly journals Time-Resolved FTIR Difference Spectroscopy Reveals the Structure and Dynamics of Carotenoid and Chlorophyll Triplets in Photosynthetic Light-Harvesting Complexes

10.5772/36178 ◽  
2012 ◽  
Author(s):  
Alexandre Maxime ◽  
Rienk van
Keyword(s):  
Light Harvesting ◽  
Difference Spectroscopy ◽  
Light Harvesting Complexes ◽  
Time Resolved ◽  
Structure And Dynamics ◽  
Ftir Difference Spectroscopy

Time-Resolved FTIR Difference Spectroscopy of Photosynthetic Bacterial Reaction Centers

1992 ◽  
pp. 79-82 ◽  
Author(s):  
D. L. Thibodeau ◽  
E. Nabedryk ◽  
R. Hienerwadel ◽  
F. Lenz ◽  
W. Mäntele ◽  
...  
Keyword(s):  
Reaction Centers ◽  
Difference Spectroscopy ◽  
Time Resolved ◽  
Bacterial Reaction Centers ◽  
Ftir Difference Spectroscopy

scholarly journals Light-Induced Infrared Difference Spectroscopy in the Investigation of Light Harvesting Complexes

Molecules ◽  
2015 ◽  
Vol 20 (7) ◽  
pp. 12229-12249 ◽  
Author(s):  
Alberto Mezzetti
Keyword(s):  
Light Harvesting ◽  
Difference Spectroscopy ◽  
Light Harvesting Complexes

scholarly journals Trimeric Photosystem I facilitates energy transfer from phycobilisomes in Synechocystis PCC 6803

2021 ◽  
Author(s):  
Parveen Akhtar ◽  
Avratanu Biswas ◽  
Fanny Balog-Vig ◽  
Ildiko Domonkos ◽  
László Kovács ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Light Harvesting ◽  
Excitation Energy Transfer ◽  
State Transitions ◽  
Synechocystis Pcc 6803 ◽  
Light Harvesting Complexes ◽  
Time Resolved ◽  
Cyanobacterial Species ◽  
In Cells ◽  
Pcc 6803

In cyanobacteria, phycobilisomes serve as peripheral light-harvesting complexes of the two photosystems, extending their antenna size and the wavelength range of photons available for photosynthesis. The abundance of phycobilisomes, the number of phycobiliproteins they contain, and their light-harvesting function are dynamically adjusted in response to the physiological conditions. Phycobilisomes are also thought to be involved in state transitions that maintain the excitation balance between the two photosystems. Unlike its eukaryotic counterpart, PSI is trimeric in many cyanobacterial species and the physiological significance of this is not well understood. Here we compared the composition and light-harvesting function of phycobilisomes in cells of Synechocystis PCC 6803, which has primarily trimeric PSI, and the ?psaL mutant unable to form trimers. We also investigated a mutant additionally lacking the PsaJ and PsaF subunits of PSI, as PsaF has been proposed to facilitate interaction with phycobilisomes. Both strains with monomeric PSI accumulated significantly less phycocyanin (which constitutes the phycobilisome rods) per chlorophyll, while the allophycocyanin content was unchanged compared to WT. These data show that cells with monomeric PSI have higher abundance of smaller phycobilisomes. Steady-state and time-resolved fluorescence spectroscopy at room temperature and 77 K revealed that PSII receives more energy from the phycobilisomes at the expense of PSI in cells with monomeric PSI, regardless of the presence of PsaF. Taken together, these results show that the trimeric organization of PSI is advantageous for efficient and balanced excitation energy transfer from phycobilisomes in Synechocystis.

scholarly journals Metal-Enhanced Fluorescence of Chlorophylls in Light-Harvesting Complexes Coupled to Silver Nanowires

2013 ◽  
Vol 2013 ◽  
pp. 1-12 ◽  
Author(s):  
Dorota Kowalska ◽  
Bartosz Krajnik ◽  
Maria Olejnik ◽  
Magdalena Twardowska ◽  
Nikodem Czechowski ◽  
...  
Keyword(s):  
Light Harvesting ◽  
Protein Complexes ◽  
Silver Nanowires ◽  
Reference Sample ◽  
Fluorescence Emission ◽  
Enhanced Fluorescence ◽  
Metal Enhanced Fluorescence ◽  
Light Harvesting Complexes ◽  
Time Resolved ◽  
Chlorophyll Protein

We investigate metal-enhanced fluorescence of peridinin-chlorophyll protein coupled to silver nanowires using optical microscopy combined with spectrally and time-resolved fluorescence techniques. In particular we study two different sample geometries: first, in which the light-harvesting complexes are deposited onto silver nanowires, and second, where solution of both nanostructures are mixed prior deposition on a substrate. The results indicate that for the peridinin-chlorophyll complexes placed in the vicinity of the silver nanowires we observe higher intensities of fluorescence emission as compared to the reference sample, where no nanowires are present. Enhancement factors estimated for the sample where the light-harvesting complexes are mixed together with the silver nanowires prior deposition on a substrate are generally larger in comparison to the other geometry of a hybrid nanostructure. While fluorescence spectra are identical both in terms of overall shape and maximum wavelength for peridinin-chlorophyll-protein complexes both isolated and coupled to metallic nanostructures, we conclude that interaction with plasmon excitations in the latter remains neutral to the functionality of the biological system. Fluorescence transients measured for the PCP complexes coupled to the silver nanowires indicate shortening of the fluorescence lifetime pointing towards modifications of radiative rate due to plasmonic interactions. Our results can be applied for developing ways to plasmonically control the light-harvesting capability of photosynthetic complexes.

scholarly journals Quinones in the A1 binding site in photosystem I studied using time-resolved FTIR difference spectroscopy

2017 ◽  
Vol 1858 (9) ◽  
pp. 804-813 ◽  
Author(s):  
Hiroki Makita ◽  
Leyla Rohani ◽  
Nan Zhao ◽  
Gary Hastings
Keyword(s):  
Binding Site ◽  
Photosystem I ◽  
Difference Spectroscopy ◽  
Time Resolved ◽  
Ftir Difference Spectroscopy

Intramolecular protein reactions investigated by time-resolved FTIR difference spectroscopy

1989 ◽  
Vol 333 (7) ◽  
pp. 778-778
Author(s):  
Klaus Gerwert ◽  
Benno Hess
Keyword(s):  
Difference Spectroscopy ◽  
Time Resolved ◽  
Ftir Difference Spectroscopy

Investigation of intramolecular processes in proteins by time resolved FTIR-difference spectroscopy

1988 ◽  
Vol 94 (1-6) ◽  
pp. 255-258 ◽  
Author(s):  
Klaus Gerwert ◽  
Benno Hess
Keyword(s):  
Difference Spectroscopy ◽  
Time Resolved ◽  
Ftir Difference Spectroscopy

scholarly journals Probing the Protein-Protein Signaling Mechanism in Intact Archaeal Cells Using Time-Resolved FTIR Difference Spectroscopy

2010 ◽  
Vol 98 (3) ◽  
pp. 560a
Author(s):  
Vladislav B. Bergo ◽  
Erica C. Saint Clair ◽  
Elena N. Spudich ◽  
John L. Spudich ◽  
Kenneth J. Rothschild
Keyword(s):  
Protein Signaling ◽  
Difference Spectroscopy ◽  
Signaling Mechanism ◽  
Time Resolved ◽  
Ftir Difference Spectroscopy
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