scholarly journals Processing of the Precursors for the Light-Harvesting Chlorophyll-Binding Proteins of Photosystem II and Photosystem I during Import and in an Organelle-Free Assay

1992 ◽  
Vol 98 (2) ◽  
pp. 595-601 ◽  
Author(s):  
Steven E. Clark ◽  
Gayle K. Lamppa
Keyword(s):  
Photosystem Ii ◽  
Photosystem I ◽  
Binding Proteins ◽  
Light Harvesting

On the question of the light-harvesting role of β-carotene in photosystem II and photosystem I core complexes

2014 ◽  
Vol 81 ◽  
pp. 121-127 ◽  
Author(s):  
Kostas Stamatakis ◽  
Merope Tsimilli-Michael ◽  
George C. Papageorgiou
Keyword(s):  
Photosystem Ii ◽  
Photosystem I ◽  
Light Harvesting ◽  
Β Carotene

scholarly journals Spatial relationship of photosystem I, photosystem II, and the light-harvesting complex in chloroplast membranes.

1977 ◽  
Vol 73 (2) ◽  
pp. 400-418 ◽  
Author(s):  
P A Armond ◽  
L A Staehelin ◽  
C J Arntzen
Keyword(s):  
Particle Size ◽  
Photosystem Ii ◽  
Photosystem I ◽  
Light Harvesting ◽  
Particle Density ◽  
Unit Size ◽  
Fracture Face ◽  
Photosynthetic Unit ◽  
Light Harvesting Complex ◽  
Chloroplast Membrane

We have previously demonstrated (Armond, P. A., C. J. Arntzen, J.-M. Briantais, and C. Vernotte. 1976. Arch. Biochem. Biophys. 175:54-63; and Davis, D. J., P. A. Armond, E. L. Gross, and C. J. Arntzen. 1976. Arch. Biochem. Biophys. 175:64-70) that pea seedlings which were exposed to intermittent illumination contained incompletely developed chloroplasts. These plastids were photosynthetically competent, but did not contain grana. We now demonstrate that the incompletely developed plastids have a smaller photosynthetic unit size; this is primarily due to the absence of a major light-harvesting pigment-protein complex which is present in the mature membranes. Upon exposure of intermittent-light seedlings to continuous white light for periods up to 48 h, a ligh-harvesting chlorophyll-protein complex was inserted into the chloroplast membrane with a concomitant appearance of grana stacks and an increase in photosynthetic unit size. Plastid membranes from plants grown under intermediate light were examined by freeze-fracture electron microscopy. The membrane particles on both the outer (PF) and inner (EF) leaflets of the thylakoid membrane were found to be randomly distributed. The particle density of the PF fracture face was approx. four times that of the EF fracture face. While only small changes in particle density were observed during the greening process under continuous light, major changes in particle size were noted, particularly in the EF particles of stacked regions (EFs) of the chloroplast membrane. Both the changes in particle size and an observed aggregation of the EF particles into the newly stacked regions of the membrane were correlated with the insertion of light-harvesting pigment-protein into the membrane. Evidence is presented for identification of the EF particles as the morphological equivalent of a "complete" photosystem II complex, consisting of a phosochemically active "core" complex surrounded by discrete aggregates of the light-harvesting pigment protein. A model demonstrating the spatial relationships of photosystem I, photosystem II, and the light-harvesting complex in the chloroplast membrane is presented.

Acclimation of the Photosynthetic Apparatus to Photosystem I or Photosystem II Light: Evidence from Quantum Yield Measurements and Fluorescence Spectroscopy of Cyanobacterial Cells

1989 ◽  
Vol 44 (1-2) ◽  
pp. 109-118 ◽  
Author(s):  
Anastasios Melis ◽  
Conrad W. Mullineaux ◽  
John F. Allen
Keyword(s):  
Quantum Yield ◽  
Photosystem Ii ◽  
Excitation Energy ◽  
Oxygen Evolution ◽  
Photosystem I ◽  
Light Harvesting ◽  
Ps Ii ◽  
Ps I ◽  
Synechococcus 6301 ◽  
Light Harvesting Antenna

Abstract Cells of the cyanobacterium Synechococcus 6301 were grown under illumination whose spectral composition favoured absorption either by the phycobilisome (PBS) light-harvesting antenna of photosystem II (PS II) or by the chlorophyll (Chi) a light-harvesting antenna of photosystem I (PS I). Cells grown under PS I-light developed relatively high PS II/PS I and PBS/Chl ratios. Cells grown under PS II-light developed relatively low PS II/PS I and PBS/Chl ratios. Thus, the primary difference between cells in the two acclimation states appeared to be the relative concentration of PBS-PS II and PS I complexes in the thylakoid membrane. Measurements of the quantum yield of oxygen evolution suggested a higher efficiency of cellular photosynthesis upon the adjustment of photosystem stoichiometry to a specific light condition. The quantum yield of oxygen evolution was nevertheless lower under PBS than Chi excitation, suggesting quenching of excitation energy in the photochemical apparatus of PS II in Synechococcus 6301. This phenomenon was more pronounced in the PS II-light than in the PS I-light grown cells. Room temperature and 77 K fluorescence emission spectroscopy indicated that excess excitation energy in the PBS was not transferred to PS I, suggesting the operation of a non-radiative and non-photochemical decay of excitation energy at the PBS-PS II complex. This non-photochemical quenching was specific to conditions where excitation of PS II occurred in excess of its capacity for useful photochemistry.

Immunological Evidence for the Binding of β-Carotene and Xanthophylls onto Peptides of Photosystem I from Nicotiana tabacum

1994 ◽  
Vol 49 (7-8) ◽  
pp. 427-438 ◽  
Author(s):  
A. Makewicz ◽  
A. Radunz ◽  
G. H. Schmid
Keyword(s):  
Nicotiana Tabacum ◽  
Photosystem Ii ◽  
Western Blot ◽  
Photosystem I ◽  
Light Harvesting ◽  
Wild Type ◽  
The Core ◽  
Ps I ◽  
Molecular Masses ◽  
Β Carotene

Photosystem I preparations were obtained from wild type tobacco Nicotiana tabacum var. John William’s Broadleaf (JWB) and from the two chlorophyll-deficient mutants N. tabacum Su/su and N. tabacum Su/su var. Aurea. The preparations were characterized with respect to the chlorophyll a/b ratio, their photosynthetic activity and their absorption spectroscopic properties. Peptides from these preparations were analyzed by SDS polyacrylamide gel electrophoresis and transferred for the detection of bound carotenoids according to the Western blot procedure to nitrocellulose or Immobilon membranes. The PS I preparation from the wild type JWB consisted of the core and the LHCP complex. The core complex contains the two core peptides with the same apparent MW of 66 kDa and several peptides with the lesser molecular masses of 22, 20, 19, 17, 16, 10 and 9 kDa. The light-harvesting protein complex consists of 4 subunits with the molecular masses 28, 26, 25 and 24 kDa. The PS I preparations of the yellow-green mutant Su/su and of the Aurea mutant Su/su var. Aurea contain as impurity traces of the D1 and D2 core peptides of photosystem II and also traces of the chlorophyll-binding photosystem II peptides with the molecular masses 42 and 47 kDa. The peptides of the photosystem I preparation were characterized by specific photosystem I antisera: An antiserum to the photosystem I complex reacts in the Western blot only with the homologous peptides of photosystem I. In comparative analyses with photosystem II preparations this antiserum (directed to photosystem I) reacts, as expected, only with the peptides of the light-harvesting complex. An antiserum to the CP 1 core peptides reacts only with the 66 kDa peptides of photosystem I and gives no cross reaction with heterodimer forms of the D1/D2 core peptides of photosystem II. In the Western blot procedure by means of polyclonal monospecific antisera to carotenoids it was demonstrated that β-carotene is bound in high concentration onto the core peptides CP 1 and to a lesser extent onto the two larger subunits of the LHCP complex, exhibiting the molecular masses of 28 and 26 kDa. Neoxanthin is bound onto the same peptides. In contrast to this, lutein was only identified on the core peptides CP 1 and violaxanthin only on the larger subunits of the LHCP complex. As the carotenoids are labelled with antibodies, even after SDS treatment in the electrophoresis, it is assumed, that the carotenoids are covalently bound via the ionon ring to the respective peptide

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