Chlorophyll-protein-complexes of thylakoids of wild type and chlorophyll b mutants of Arabidopsis thaliana

1983 ◽  
Vol 4 (4) ◽  
pp. 301-305 ◽  
Author(s):  
Wolfgang R�hle ◽  
Helmut Reil�nder ◽  
Klaus-Dieter Otto ◽  
Aloysius Wild
Keyword(s):  
Arabidopsis Thaliana ◽  
Protein Complexes ◽  
Chlorophyll B ◽  
Wild Type ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein

Chlorophyll-protein-complexes of thylakoids of wild type and chlorophyll b mutants of Arabidopsis thaliana

1983 ◽  
Vol 4 (1) ◽  
pp. 301-305 ◽  
Author(s):  
Wolfgang R�hle ◽  
Helmut Reil�nder ◽  
Klaus -Dieter Otto ◽  
Aloysius Wild
Keyword(s):  
Arabidopsis Thaliana ◽  
Protein Complexes ◽  
Chlorophyll B ◽  
Wild Type ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein

Chlorophyll-Protein Complexes of Chlorella fusca

1980 ◽  
Vol 35 (7-8) ◽  
pp. 627-637 ◽  
Author(s):  
Aloysius Wild ◽  
Barbara Urschel
Keyword(s):  
Chlorophyll A ◽  
Light Harvesting ◽  
Protein Complexes ◽  
Sodium Dodecyl ◽  
Chlorophyll B ◽  
Chlorella Fusca ◽  
Ps Ii ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein ◽  
Set Up

Chlorophyll-protein complexes from thylakoids of the normal type and two mutants of Chlorella fusca were separated using sodium dodecyl sulfate acrylamide gel electrophoresis (PAGE). The properties of the chlorophyll-protein complexes of the three strains of Chlorella were compared. Standard curves were set up for the characterization of the chlorophyll-proteins. In every electrophoretic separation of chlorophyll-protein complexes, a certain amount of pigment is separated from the protein. We tried to keep that amount as low as possible by mild solubiliza­tion and by working in low temperature. Under these conditions, we obtained several new chlorophyll-proteins in addition to the P-700-chlorophyll a-protein (CP I) and the light-harvesting chlorophyll a/b-protein (CP II). Thus, a small band (CP I a) was located between the top of the gel and the CPI after elec­trophoresis. Although it shows spectral qualities similar to CP I, it possesses a much lower chloro­phyll a/chlorophyll b ratio. It may be an aggregate of photosystem I and light-harvesting chloro­phyll. We found and analyzed three other chlorophyll-proteins with electrophoretic mobilities inter­mediate between that of the P-700-chlorophyll a-protein and that of the light-harvesting chloro­phyll a/b-protein complex. Two of these chlorophyll-proteins, the LHCP1 and the LHCP2, have a low chlorophyll a/chlorophyll b ratio and spectral properties similar to that of the light-harvesting chlorophyll a/b-protein (LHCP3). They obviously represent dimers or oligomers of the latter com­plex. A third, new complex (CPa) migrated between LHCP3 and its dimer. With the chlorophyll b deficient mutant G 36 of Chlorella fusca, this complex could be obtained in high purity and great enrichment (15% of total chlorophyll). It could be proved that this complex only contains chloro­phyll a. Its red absorption maximum is at 671 nm. Some indirect evidences suggest that it may be a good candidate for the PS II reaction center complex.

scholarly journals Chiroptical properties of chlorophyll-protein complexes separated on Deriphat/polyacrylamide gel

1982 ◽  
Vol 202 (1) ◽  
pp. 25-29 ◽  
Author(s):  
R P F Gregory ◽  
G Borbély ◽  
S Demeter ◽  
A Faludi-Dániel
Keyword(s):  
Chlorophyll A ◽  
Protein Complexes ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Chlorophyll B ◽  
Chlorophyll Protein Complexes ◽  
New Type ◽  
Chlorophyll Protein ◽  
Zwitterionic Detergent ◽  
Exciton Type

Circular dichroism (c.d.) was measured for four chlorophyll-protein complexes, resolved from sodium dodecyl sulphate extracts of chloroplasts by electrophoresis in polyacrylamide gel containing Deriphat 160 (disodium N-dodecyl beta-imidopropionate), a zwitterionic detergent. The slowest-band (1) complex was found to be identical with the complex CP1 as found on electrophoresis in the presence of anion detergent, but it was in a much higher yield (30% of the chlorophyll a). In band-2 and -3 protein complexes a c.d. pattern described for the complex CP2 could be recognized. Another c.d. component of a split-exciton type with extrema at 680 (-) and 669 (+)nm, together with evidence of disorganized chlorophyll, was found in band-2, -3 and -4 complexes. When a barley (Hordeum vulgare) mutant lacking chlorophyll b was examined, only bands 1 and 4 were obtained, and the c.d. of the band-4 complex was much less affected by disorganized chlorophyll. C.D. spectra resembling that of this band-4 complex could be generated by subtracting the c.d. of complex CP1 from the c.d. of photochemically active mutant chloroplast fragments, or by subtracting the c.d. of complexes CP1 and CP2 from pea (Pisum sativum) chloroplast fragments. The Deriphat appears to have preserved at least to some extent a new type of chlorophyll a-protein complex.

scholarly journals The Arabidopsis Accessions Selection Is Crucial: Insight from Photosynthetic Studies

2021 ◽  
Vol 22 (18) ◽  
pp. 9866
Author(s):  
Joanna Wójtowicz ◽  
Katarzyna B. Gieczewska
Keyword(s):  
Arabidopsis Thaliana ◽  
Protein Complexes ◽  
Photosynthetic Apparatus ◽  
Adaptive Plasticity ◽  
Natural Genetic Variation ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein ◽  
Pigment Distribution ◽  
Photosynthetic Machinery ◽  
Characteristic Features

Natural genetic variation in photosynthesis is strictly associated with the remarkable adaptive plasticity observed amongst Arabidopsis thaliana accessions derived from environmentally distinct regions. Exploration of the characteristic features of the photosynthetic machinery could reveal the regulatory mechanisms underlying those traits. In this study, we performed a detailed characterisation and comparison of photosynthesis performance and spectral properties of the photosynthetic apparatus in the following selected Arabidopsis thaliana accessions commonly used in laboratories as background lines: Col-0, Col-1, Col-2, Col-8, Ler-0, and Ws-2. The main focus was to distinguish the characteristic disparities for every accession in photosynthetic efficiency that could be accountable for their remarkable plasticity to adapt. The biophysical and biochemical analysis of the thylakoid membranes in control conditions revealed differences in lipid-to-protein contribution, Chlorophyll-to-Carotenoid ratio (Chl/Car), and xanthophyll cycle pigment distribution among accessions. We presented that such changes led to disparities in the arrangement of the Chlorophyll-Protein complexes, the PSI/PSII ratio, and the lateral mobility of the thylakoid membrane, with the most significant aberrations detected in the Ler-0 and Ws-2 accessions. We concluded that selecting an accession suitable for specific research on the photosynthetic process is essential for optimising the experiment.

Photoinhibition in vivo and in vitro Involves Weakly Coupled Chlorophyll–Protein Complexes‡¶

2002 ◽  
Vol 75 (6) ◽  
pp. 613 ◽  
Author(s):  
Stefano Santabarbara ◽  
Ilaria Cazzalini ◽  
Andrea Rivadossi ◽  
Flavio M. Garlaschi ◽  
Giuseppe Zucchelli ◽  
...  
Keyword(s):  
Protein Complexes ◽  
Weakly Coupled ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein
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