scholarly journals The Low-Energy Forms of Photosystem I Light-Harvesting Complexes: Spectroscopic Properties and Pigment-Pigment Interaction Characteristics

2007 ◽  
Vol 93 (7) ◽  
pp. 2418-2428 ◽  
Author(s):  
Roberta Croce ◽  
Agnieszka Chojnicka ◽  
Tomas Morosinotto ◽  
Janne A. Ihalainen ◽  
Frank van Mourik ◽  
...  
Keyword(s):  
Photosystem I ◽  
Light Harvesting ◽  
Spectroscopic Properties ◽  
Low Energy ◽  
Light Harvesting Complexes

Ultrafast excitation dynamics of low energy pigments in reconstituted peripheral light-harvesting complexes of photosystem I

FEBS Letters ◽  
2000 ◽  
Vol 471 (1) ◽  
pp. 89-92 ◽  
Author(s):  
Alexander N. Melkozernov ◽  
Su Lin ◽  
Volkmar H.R. Schmid ◽  
Harald Paulsen ◽  
Gregory W. Schmidt ◽  
...  
Keyword(s):  
Photosystem I ◽  
Light Harvesting ◽  
Low Energy ◽  
Light Harvesting Complexes ◽  
Excitation Dynamics

scholarly journals The light-harvesting complexes of higher-plant Photosystem I: Lhca1/4 and Lhca2/3 form two red-emitting heterodimers

2011 ◽  
Vol 433 (3) ◽  
pp. 477-485 ◽  
Author(s):  
Emilie Wientjes ◽  
Roberta Croce
Keyword(s):  
Photosystem I ◽  
Light Harvesting ◽  
Fluorescence Emission ◽  
Light Response ◽  
Native State ◽  
Higher Plant ◽  
Light Harvesting Complexes ◽  
Light Harvesting Complex ◽  
Wavelength Emission

The outer antenna of higher-plant PSI (Photosystem I) is composed of four complexes [Lhc (light-harvesting complex) a1–Lhca4] belonging to the light-harvesting protein family. Difficulties in their purification have so far prevented the determination of their properties and most of the knowledge about Lhcas has been obtained from the study of the in vitro reconstituted antennas. In the present study we were able to purify the native complexes, showing that Lhca2/3 and Lhca1/4 form two functional heterodimers. Both dimers show red-fluorescence emission with maxima around 730 nm, as in the intact PSI complex. This indicates that the dimers are in their native state and that LHCI-680, which was previously assumed to be part of the PSI antenna, does not represent the native state of the system. The data show that the light-harvesting properties of the two dimers are functionally identical, concerning absorption, long-wavelength emission and fluorescence quantum yield, whereas they differ in their high-light response. Implications of the present study for the understanding of the energy transfer process in PSI are discussed. Finally, the comparison of the properties of the native dimers with those of the reconstituted complexes demonstrates that all of the major properties of the Lhcas are reproduced in the in vitro systems.

Charge-Transfer Character of the Low-Energy Chl a Qy Absorption Band in Aggregated Light Harvesting Complexes II

2014 ◽  
Vol 118 (23) ◽  
pp. 6086-6091 ◽  
Author(s):  
Adam Kell ◽  
Ximao Feng ◽  
Chen Lin ◽  
Yiqun Yang ◽  
Jun Li ◽  
...  
Keyword(s):  
Charge Transfer ◽  
Absorption Band ◽  
Light Harvesting ◽  
Low Energy ◽  
Light Harvesting Complexes ◽  
Chl A

Isolation and characterization of three membranebound chlorophyll-protein complexes from four dinoflagellate species

1993 ◽  
Vol 340 (1294) ◽  
pp. 381-392 ◽  
Keyword(s):  
Energy Transfer ◽  
Photosystem I ◽  
Light Harvesting ◽  
Protein Complexes ◽  
Gradient Centrifugation ◽  
Water Soluble ◽  
Molar Ratio ◽  
Light Harvesting Complexes ◽  
Light Harvesting Complex ◽  
Isolation And Characterization

Employing discontinuous sucrose density gradient centrifugation of n -dodecyl β-d-maltoside-solubilized thylakoid membranes, three chlorophyll (Chl)-protein complexes containing Chl a , Chl c 2 and peridinin in different proportions, were isolated from the dinoflagellates Symbiodinium microadriaticum, S. kawagutii, S. pilosum and Heterocapsa pygmaea . In S. microadriaticum , the first complex, containing 13% of the total cellular Chl a , and minor quantities of Chl c 2 and peridinin, is associated with polypeptides with apparent molecular mass ( M r ) of 8-9 kDa, and demonstrated inefficient energy transfer from the accessory pigments to Chl a . The second complex contains Chl a , Chl c 2 and peridinin in a molar ratio of 1:1:2, associated with two apoproteins of M r 19-20 kDa, and comprises 45%, 75% and 70%, respectively, of the cellular Chl a , Chl c 2 and peridinin. The efficient energy transfer from Chl c 2 and peridinin to Chl a in this complex is supportive of a light-harvesting function. This Chl a - c 2 - peridin-protein complex represents the major light-harvesting complex in dinoflagellates. The third complex obtained contains 12% of the cellular Chl a , and appears to be the core of photosystem I, associated with a light-harvesting complex. This complex is spectroscopically similar to analogous preparations from different taxonomic groups, but demonstrates a unique apoprotein composition. Antibodies against the water-soluble peridinin-Chl a -protein (sPCP) light-harvesting complexes failed to cross-react with any of the thylakoid-associated complexes, as did antibodies against Chl a - c -fucoxanthin apoprotein (from diatoms). Antibodies against the P 700 apoprotein of plants did not cross-react with the photosystem I complex. Similar results were observed in the other dinoflagellates.

scholarly journals Functional analysis of Photosystem I light-harvesting complexes (Lhca) gene products of Chlamydomonas reinhardtii

2010 ◽  
Vol 1797 (2) ◽  
pp. 212-221 ◽  
Author(s):  
Milena Mozzo ◽  
Manuela Mantelli ◽  
Francesca Passarini ◽  
Stefano Caffarri ◽  
Roberta Croce ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Chlamydomonas Reinhardtii ◽  
Photosystem I ◽  
Light Harvesting ◽  
Gene Products ◽  
Light Harvesting Complexes
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