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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Photosynthesis research 11 (1987), S. 29-36 
    ISSN: 1573-5079
    Keywords: β-carotene ; heptane extraction ; Photosystem I reaction center ; subunit structure ; phylloquinone (vitamin K1) ; (Synechococcus sp.)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Treatment of lyophilized thylakoid membranes of the thermophilic cyanobacterium Synechococcus sp. with n-heptane for 6 h resulted in marked changes in the pattern of photosystem I reaction center complexes resolved by sodium dodecylsulfate-polyacrylamide gel electrophoresis. CP1-a, which consists of two large subunits and three small subunits, was a major chlorophyll-containing band resolved from the lyophilized thylakoid membranes, whereas the heptane-extracted membranes produced mainly CP1-e which totally lacks the small subunits. Electron transport from the primary donor P700 to the secondary acceptor P430 was not affected by the heptane-extraction of the membranes. The heptane-treatment removed 97% of β-carotene present in the membranes, whereas all chlorophyll a, a major part of xanthophylls, more than a half of phylloquinone and one third of plastoquinone remained unextracted. The data suggest that β-carotene has an important structural effect to stabilize the subunit organization of photosystem I reaction center complexes but is not essential for the early photochemical events of photosystem I.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-5079
    Keywords: β-carotene ; iron ; photosystem I reaction center complex ; P700 ; (Synechococcus sp.) ; vitamin K1
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The iron, quinone and carotenoid contents of five P700-chlorophyll a-protein complexes having different subunit structures (CP1-a,-b,-c,-d and-e) from the thermophilic cyanobacterium Synechococcus sp. were determined. CP1-a,-b,-c and-d that commonly have four polypeptides of 62,000, 60,000, 14,000 and 10,000 dalton contained 10–14 iron atoms per P700, whereas CP1-e that lacks the two small polypeptides was totally devoid of iron. All CP1 complexes contained vitamin K1 at the molar ratio of vitamin K1 to P700 of about 2 except CP1-e that had only 0.4 vitamin K1 per P700. No plastoquinone was detected in five CP1 complexes. Out of four major carotenoids, β-carotene, zeaxanthin, caloxanthin, and myxoxanthophyll, present in the thylakoid membranes, only β-carotene was found in isolated CP1 complexes; all CP1 complexes contained about 10 β-carotene molecules per P700. The flourescence excitation spectrum showed that β-carotene serves as an efficient antenna of photosystem I. It is concluded that all iron atoms and a larger fraction of vitamin K1 molecules present in the photosystem I reaction center complex are associated with the 14,000 and 10,000 dalton polypeptides, whereas β-carotene exclusively binds to the large polypeptides which carry the functional and antenna chlorophyll a. The possible functions of iron and vitamin K1 as electron carriers and of β-carotene as the accessary pigment and a photoprotectant in the photosystem I complexes are discussed.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-5028
    Keywords: Chlamydomonas reinhardtii ; chloroplast ; transformation ; photosystem II ; psbK
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Using particle gun-mediated chloroplast transformation we have disrupted the psbK gene of Chlamydomonas reihardtii with an aadA expression cassette that confers resistance to spectinomycin. The transformants are unable to grow photoautotrophically, but they grow normally in acetate-containing medium. They are deficient in photosystem II activity as measured by fluorescence transients and O2 evolution and they accumulate less than 10% of wild-type levels of photosystem II as measured by immunochemical means. Pulse-labeling experiments indicate that the photosystem II complex is synthesized normally in the transformants. These results differ from those obtained previously with similar cyanobacterial psbK mutants that were still capable of photoautotrophic growth (Ikeuchi et al., J. Biol. Chem. 266 (1991) 1111–1115). In C. reinhardtii the psbK product is required for the stable assembly and/or stability of the photosystem II complex and essential for photoautotrophic growth. The data also suggest that the stability requirements of the photosynthetic complexes differ considerably between C. reinhardtii and cyanobacteria.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1573-5028
    Keywords: Chlamydomonas reinhardtii ; chloroplast transformation ; photosynthesis ; photosystem II ; processing ; psbA gene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract One of the photosystem II reaction center proteins, D1, is encoded by the psbA gene and is synthesized as a precursor form with a carboxyl-terminal extension that is subsequently cleaved between Ala-344 and Ser-345. We have generated three psbA transformants of the green alga Chlamydomonas reinhardtii in which Ala-344 or Ser-345 have been substituted with Pro or Glu (A344P, S345E, and S345P) to understand the effects of the amino acid substitutions on the processing of the precursor D1. S345E grew photoautotrophically and showed PSII activity like the wild type. However, A344P and S345P were unable to grow photoautotrophically and were significantly photosensitive. A344P was deficient in the processing of precursor D1 and in oxygen-evolving activity, but assembled photosystem II complex capable of charge separation. In contrast, both precursor and mature forms of D1 accumulated in S345P cells from the logarithmic phase and the cells evolved oxygen at 18% of wild-type level. However, S345P cells from the stationary phase contained mostly the mature D1 and showed a twofold increase in oxygen-evolving activity. The rate of processing of the accumulated pD1 was estimated to be about 100 times slower than in the wild type. It is therefore concluded that the functional oxygen-evolving complex is assembled when the precursor D1 is processed, albeit at a very low rate. These results suggest the functional significance of the amino acid residues at the processing site of the precursor D1.
    Type of Medium: Electronic Resource
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