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  • 1
    Electronic Resource
    Electronic Resource
    Circular dichroism and polarized fluorescence characteristics of blue-green algal allophycocyanins (1980)
    s.l. : American Chemical Society
    Biochemistry 19 (1980), S. 2950-2956 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00554a021
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  • 2
    Electronic Resource
    Electronic Resource
    Association of phycoerythrin and phycocyanin: in vitro formation of a functional energy transferring phycobilisome complex of Porphyridium sordidum (1981)
    s.l. : American Chemical Society
    Biochemistry 20 (1981), S. 3371-3376 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00515a010
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  • 3
    Electronic Resource
    Electronic Resource
    Phycobilisomes of Porphyridium cruentum. Pigment analysis (1974)
    s.l. : American Chemical Society
    Biochemistry 13 (1974), S. 2960-2966 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00711a027
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  • 4
    Electronic Resource
    Electronic Resource
    LhcaR1 of the red alga Porphyridium cruentum encodes a polypeptide of the LHCI complex with seven potential chlorophyll a-binding residues that are conserved in most LHCs (1997)
    Springer
    Plant molecular biology 33 (1997), S. 157-167 
    Details
    ISSN: 1573-5028
    Keywords: chlorophyll a-binding protein ; gene expression ; LHC ; light-harvesting complex ; photosystem I ; rhodophyte
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The accessory light-harvesting polypeptides associated with photosystem I (LHCI) in Porphyridium cruentum bind chlorophyll a, zeaxanthin and β-carotene. A cDNA library of P. cruentum was screened with an antiserum specific to the LHCI polypeptides, and an 0.9 kb fragment was identified as coding for an LHCI polypeptide. This cDNA, which we named LhcaR1, has an open reading frame encoding 222 amino acid residues including a putative transit peptide of 28 amino acids. Hydropathy analysis suggests that there are three transmembrane helices in the mature polypeptide. Each of the amino acid residues that bind chlorophyll (six residues) and serve in stabilizing the helices in higher-plant LHCs are conserved in helices 1 and 3 of P. cruentum LhcaR1. The N-terminal flanking regions of these two helices also show high sequence conservation with other LHCs. Helix 2 contains a seventh putative chlorophyll-binding site, but resembles helix 2 of higher-plant LHCs to a lesser degree. A sequence motif of 11 residues found near the N-terminus and in each of the three helices suggests the possibility that the red algal LhcaR1 derives from a gene duplication. Polypeptides of the expected molecular weight in six other red algae (Achrochaetium, Bangia, Callithamnion, Cyanidium, Polysiphonia, Spermothamnion) were recognized by the antiserum to P. cruentum LHCI, indicating a wide distribution of LHCI in rhodophytes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005715528297
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  • 5
    Electronic Resource
    Electronic Resource
    Trichodesmium thiebautii; structure of a nitrogen-fixing marine blue-green alga (Cyanophyta) (1984)
    Springer
    Protoplasma 119 (1984), S. 188-196 
    Details
    ISSN: 1615-6102
    Keywords: Electron-dense fibers ; Gas vesicles ; Thylakoids ; Trichodesmium thiebautii
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Trichodesmium thiebautii was collected, as floating bundles composed of uniseriate filaments aligned in parallel, from the Kuroshio waters off Shikoku Island, Japan. The ultrastructure of this alga had basically the same general features as the related speciesT. erythraeum first described byvan Baalen andBrown (1969). InT. thiebautii long electron dense fibers and concentrically lamellated bodies were observed which were either not reported previously, or did not occur inT. erythraeum. The peripheral wall layers were generally typical ofOscillatoria-type blue-green algae, but with a distinctive finely striated outer layer. Thylakoids per cell volume were very sparse compared to most other blue-green algae. Phycobilisomes, apparently hemidiscoidal in shape, typically occurred on the stromal side of the thylakoid surface. Large gas vesicle areas occupied the main volume of the cell, including cells which seemed to be actively growing. The gas vesicle areas were distributed throughout the cell, not only in the cell periphery as inT. erythraeum. Considerable complexity was suggested by the apparent cell compartmentation, particularly because the gas vesicle areas were delimited by one to several thylakoids. Only rarely were the gas vesicle areas traversed by thylakoids. Electron dense fibers (ca. 25 nm diameter) were always observed between the gas vesicles and were usually oriented parallel with them, but they were not rigid appearing as were the gas vesicles. The gas vesicles had a smaller diameter (ca. 45 nm) than most blue-greens. Concentrically lamellated bodies (ca. 1.0 μm diameter) were observed in cells of some of the bundles. Each concentric layer was ca. 1.3 nm wide. These concentrically lamellated bodies may be characteristic of older cells. Cylindrical bodies were considerably smaller (ca. 120 nm diameter) and less complex than those reported forT. erythraeum.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01288873
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  • 6
    Electronic Resource
    Electronic Resource
    A high molecular weight terminal pigment (“anchor polypeptide”) and a minor blue polypeptide from phycobilisomes of the cyanobacterium Nostoc sp. (MAC): Isolation and characterization (1986)
    Springer
    Photosynthesis research 10 (1986), S. 201-208 
    Details
    ISSN: 1573-5079
    Keywords: Terminal pigment ; Cyanobacteria ; Energy transfer ; Photosynthesis ; Phycobilisome ; Nostoc sp.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A 94 kD pigment-polypeptide, which is presumed to be involved in anchoring the phycobilisomes to the thylakoids, was isolated from Nostoc phycobilisomes by gel filtration in 63 mM formic acid. The isolation condition did not require detergents or denaturating reagents, as in previous procedures, and enzymatic degradation was not observed at the low pH of 2.5. The “anchor polypeptide” thus obtained had absorption (Abs) and fluorescence maxima (Em) at 658 and 673 nm, respectively, in 63 mM formic acid at room temperature. The maxima shifted to longer wavelengths in 100 mM potassium phosphate (pH 6.8), Abs 665 and Em 683 nm at room temperature, and Abs 665 and Em 684 nm at liquid nitrogen temperature. The fluorescence maxima at both temperatures correspond to the longest wavelength component resolved in phycobilisomes from second derivative spectra. A minor blue polypeptide was also found by this isolation method. The molecular weight of this polypeptide was ca. 18,000 and is probably similar to a polypeptide which has been found in the phycobilisome core of other cyanobacteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00118284
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  • 7
    Electronic Resource
    Electronic Resource
    Variation in the polypeptide composition of phycobilisomes from Anacystis nidulans and three pigment mutants (1986)
    Springer
    Photosynthesis research 8 (1986), S. 149-159 
    Details
    ISSN: 1573-5079
    Keywords: allophycocyanin ; Anacystis ; phycobilisomes ; phycocyanin ; pigment mutants polypeptides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Phycobilisomes, light harvesting antenna pigment systems, were studied from Anacystis nidulans wild type and from several spontaneous pigment mutants selected for improved growth in far-red light (〉650 nm). This is the first characterization and description of polypeptide composition of phycobilisomes from spontaneous mutants (not chemically induced) of A. nidulans. The mutants had significant changes in the phycobiliprotein content relative to chlorophyll (Chl). Two phycobiliproteins, C-phycocyanin (λmax 625 nm) and allophycocyanin (λmax 650 nm) were present in a molar ratio of ∼3:1 in the wild type. In the mutants the amount of allophycocyanin (APC) per cell remained constant but the phycocyanin (PC) content varied. Phycobilisomes of the mutants 85Y, 19Y and 59G contained PC and APC in a molar ratio of 0.4:1, 0.7:1, and 1:1, respectively. Even though the phycobilisomes of mutant 85Y showed the greatest reduction in PC and consisted mostly of the APC core, the phycobilisomes were still functional and the growth rate of the 85Y cells was similar to the wild type. Fluorescence emission maxima of wild type and all the mutants were at 680 nm (23°C). Excitation maxima corresponded closely with expectations from absorption spectra. On SDS-PAGE gradient gels wild-type phycobilisomes had the usual 17–19 kD polypeptides of PC and APC, plus polypeptides at ca. 78, 56, 39, 36 and 31 kD. Mutants 19Y and 85Y, with the greatest PC deficiency were also deficient in the 36 and 39 kD polypeptides, presumably due to a decrease in peripheral rod structures. Energetically functional hybrid phycobilisomes were obtained when complexes of phycoerythrin-phycocyanin from Nostoc were mixed with dissociated phycobilisomes of wild-type and mutant 85Y. The 31 kD polypeptide is common to both species and immunologically cross reactive.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00035245
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  • 8
    Electronic Resource
    Electronic Resource
    Characterization of the Porphyridium cruentum Chl a-binding LHC by in vitro reconstitution: LHCaR1 binds 8 Chl a molecules and proportionately more carotenoids than CAB proteins (2000)
    Springer
    Photosynthesis research 63 (2000), S. 85-96 
    Details
    ISSN: 1573-5079
    Keywords: chlorophyll a ; Chl a-binding protein ; evolution ; light-harvesting complex ; LHC I ; Porphyridium cruentum ; reconstitution ; red alga ; zeaxanthin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The Porphyridium cruentum light harvesting complex (LHC) binds Chl a, zeaxanthin and β-carotene and comprises at least 6 polypeptides of a multigene family. We describe the first in vitro reconstitution of a red algal light-harvesting protein (LHCaR1) with Chl a/carotenoid extracts from P. cruentum. The reconstituted pigment complex (rLHCaR1) is spectrally similar to the native LHC I, with an absorption maximum at 670 nm, a 77 K fluorescence emission peak at 677 nm (ex. 440 nm), and similar circular dichroism spectra. Molar ratios of 4.0 zeaxanthin, 0.3 β-carotene and 8.2 Chl a per polypeptide for rLHCaR1 are similar to those of the native LHC I complex (3.1 zeaxanthin, 0.5 β-carotene, 8.5 Chl a). The binding of 8 Chl a molecules per apoprotein is consistent with 8 putative Chl-binding sites in the predicted transmembrane helices of LHCaR1. Two of the putative Chl a binding sites (helix 2) in LHCaR1 were assigned to Chl b in Chl a/b-binding (CAB) LHC II [Kühlbrandt et al. (1994) Nature 367: 614–21]. This suggests either that discrimination for binding of Chl a or Chl b is not very specific at these sites or that specificity of binding sites evolved separately in CAB proteins. LHCaR1 can be reconstituted with varying ratios of carotenoids, consistent with our previous observation that the carotenoid to Chl ratio is substantially higher in P. cruentum grown under high irradiance. Also notable is that zeaxanthin does not act as an accessory light-harvesting pigment, even though it is highly likely that it occupies the position assigned to lutein in the CAB LHCs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006357107247
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  • 9
    Electronic Resource
    Electronic Resource
    Pigment orientation changes accompanying the light state transition in Synechococcus sp. PCC 6301 (1994)
    Springer
    Photosynthesis research 40 (1994), S. 35-44 
    Details
    ISSN: 1573-5079
    Keywords: allophycocyanin ; chlorophyll a ; linear dichroism ; phycobilisome ; photosynthesis ; state transition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Low temperature (77 K) linear dichroism spectroscopy was used to characterize pigment orientation changes accompanying the light state transition in the cyanobacterium, Synechococcus sp. PCC 6301 and those accompanying chromatic acclimation in Porphyridium cruentum in samples stabilized by glutaraldehyde fixation. In light state 2 compared to light state 1 intact cells of Synechococcus showed an increased alignment of allophycocyanin parallel to the cells' long axis whereas the phycobilisomethylakoid membrane fragments exhibited an increased allophycocyanin alignment parallel to the membrane plane. The phycobilisome-thylakoid membrane fragments showed less alignment of a short wave-length chlorophyll a (Chl a) Qy transition dipole parallel to the membrane plane in state 2 relative to state 1. To aid identification of the observed Chl a orientation changes in Synechococcus, linear dichroism spectra were obtained from phycobilisome-thylakoid membrane fragments isolated from red light-grown (increased number of PS II centres) and green light-grown (increased number of PS I centres) cells of the red alga Porphyridium cruentum. An increased contribution of short wavelength Chl a Qy transition dipoles parallel to the long axis of the membrane plane was directly correlated with increased levels of PS II centres in red light-grown P. cruentum. Our results indicate that the transition to state 2 in cyanobacteria is accompanied by an increase in the orientation of allophycocyanin and a decrease in the orientation of Chl a associated with PS II with respect to the thylakoid membrane plane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00019043
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  • 10
    Electronic Resource
    Electronic Resource
    Decrease of polypeptides in the PS I antenna complex with increasing growth irradiance in the red alga Porphyridium cruentum (1995)
    Springer
    Photosynthesis research 45 (1995), S. 1-10 
    Details
    ISSN: 1573-5079
    Keywords: light-harvesting antenna ; Mehler reaction ; Photosystem I ; Porphyridium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Thylakoids isolated from cells of the red alga Porphyridium cruentum exhibit an increased PS I activity on a chlorophyll basis with increasing growth irradiance, even though the stoichiometry of Photosystems I and II in such cells shows little change (Cunningham et al. (1989) Plant Physiol 91: 1179–1187). PS I activity was 26% greater in thylakoids of cells acclimated at 280 μmol photons · m−2 · s−1 (VHL) than in cells acclimated at 10 μmol photons · m−2 · s−1 (LL), indicating a change in the light absorbance capacity of PS I. Upon isolating PS I holocomplexes from VHL cells it was found that they contained 132±9 Chl/P700 while those obtained from LL cells had 165±4 Chl/P700. Examination of the polypeptide composition of PS I holocomplexes on SDS-PAGE showed a notable decrease of three polypeptides (19.5, 21.0 and 22 kDa) in VHL-complexes relative to LL-complexes. These polypeptides belong to a novel LHC I complex, recently discovered in red algae (Wolfe et al. (1994a) Nature 367: 566–568), that lacks Chl b and includes at least six different polypeptides. We suggest that the decrease in PS I Chl antenna size observed with increasing irradiance is attributable to changes occurring in the LHC I-antenna complex. Evidence for a Chl-binding antenna complex associated with PS II core complexes is lacking at this point. LHC II-type polypeptides were not observed in functionally active PS II preparations (Wolfe et al. (1994b) Biochimica Biophysica Acta 1188: 357–366), nor did we detect polypeptides that showed immunocross-reactivity with LHC II specific antisera (made to Chlamydomonas and Euglena LHC II).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00032230
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