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.

Variabilität des "light-harvesting-systems" im Zellzyklus von Chlorella fusca / Variability of the Light-Harvesting-System during the Cell Cycle of Chlorella fusca

1985 ◽  
Vol 40 (1-2) ◽  
pp. 115-121 ◽  
Author(s):  
Peter Brandt ◽  
Helene Gleibs ◽  
Andrea Kohne ◽  
Wolfgang Wiessner
Keyword(s):  
Cell Cycle ◽  
Light Harvesting ◽  
Higher Plants ◽  
Protein Complexes ◽  
Light Period ◽  
Chlorella Fusca ◽  
Chlorophyll Accumulation ◽  
Harvesting Systems ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein

The seven chlorophyll-protein complexes CPIa, CPI, LHCP1, LHCP2, CPa, LHCP1 and LHCP11 known in part also from the chloroplasts of higher plants were isolated from Chlorella fusca. They were characterized by their molecular weight, their absorption maxima and their ratio of chlorophyll a/chlorophyll b. The composition of the chloropyhll-protein complexes changes during the cell cycle of Chlorella fusca. The ratio of LHCP/CPI decreases at the beginning of the light period and the ratio LHCP/CPa after the 2nd hour of the light period. Both quotients increase at the 5th hour of the light period, have a maximum at the 8th hour of the light period and decrease afterwards during the second part of the cell cycle. These altera­tions are no reflections of chlorophyll-accumulation, but cause modifications in the organization of the thylakoids and influence the photosynthetic efficiency of Chlorella fusca. The size of the PSI- and PSII-units during the cell cycle was estimated by these changes of the LHCP/CPI- and LHCP/CPa-ratios. In addition evidence is given that the assembly of LHCP1 and LHCP2 is no simple association of the monomeric forms of LHCPI or LHCPII.

Construction of a Porphyrin-Based Nanohybrid as an Analogue of Chlorophyll Protein Complexes and Its Light-Harvesting Behavior Research

2016 ◽  
Vol 120 (2) ◽  
pp. 919-926 ◽  
Author(s):  
Xingming Ning ◽  
Liang Ma ◽  
Shouting Zhang ◽  
Dongdong Qin ◽  
Duoliang Shan ◽  
...  
Keyword(s):  
Light Harvesting ◽  
Protein Complexes ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein

Growth and development at cold-hardening temperatures. Chlorophyll–protein complexes and thylakoid membrane polypeptides

1984 ◽  
Vol 62 (1) ◽  
pp. 61-67 ◽  
Author(s):  
B. Elfman ◽  
N. P. A. Huner ◽  
M. Griffith ◽  
M. Krol ◽  
W. G. Hopkins ◽  
...  
Keyword(s):  
Growth And Development ◽  
Light Harvesting ◽  
Protein Complexes ◽  
Thylakoid Membranes ◽  
Cold Hardening ◽  
Complex Iv ◽  
Light Harvesting Complex ◽  
Dodecyl Sulfate ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein

Chlorophyll–protein complexes of thylakoid membranes from rye plants (Secale cereale L. cv. Puma) grown at warm and cold-hardening temperatures were investigated by gel electrophoresis. Complex IV from cold-grown tissue was detectable in the presence of dodecyl sulfate if and only if solubilization and electrophoresis were performed at 4 °C, whereas complex IV from warm-grown material was detectable if membrane solubilization and electrophoresis were performed at either 4 or 23 °C in the presence of dodecyl sulfate. In the presence of octyl-β-D-glucopyranoside, the chlorophyll–protein complexes from cold-grown tissue were less stable at 23 °C than those from warm-grown tissue. Regardless of the detergent used, there was always more oligomer of the light-harvesting complex present in samples prepared from thylakoid membranes of warm-grown tissue than those from membranes of cold-grown tissue. It is concluded that the pigment–protein interaction in those complexes associated with photosystem II and the light-harvesting chlorophyll a/b – protein complex has been altered upon growth and development at cold-hardening temperatures.

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