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  • 1
    Electronic Resource
    Electronic Resource
    Structure, Function, and Mutational Analysis of V-ATPases (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 671 (1992), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1992.tb43803.x
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  • 2
    Electronic Resource
    Electronic Resource
    Crystal structure of plant photosystem I (2003)
    [s.l.] : Macmillian Magazines Ltd.
    Nature 426 (2003), S. 630-635 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Oxygenic photosynthesis is the principal producer of both oxygen and organic matter on Earth. The conversion of sunlight into chemical energy is driven by two multisubunit membrane protein complexes named photosystem I and II. We determined the crystal structure of the complete photosystem I (PSI) ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature02200
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  • 3
    Electronic Resource
    Electronic Resource
    The atp1 and atp2 operons of the cyanobacterium Synechocystis sp. PCC 6803 (1991)
    Springer
    Plant molecular biology 17 (1991), S. 641-652 
    Details
    ISSN: 1573-5028
    Keywords: F-ATPase ; cyanobacteria ; operon ; evolution ; photosynthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The two operons atp1 and atp2, encoding the subunits of the FOF1 ATP-synthase, have been cloned and sequenced from the cyanobacterium Synechocystis sp. PCC 6803. The organization of the different genes in the operons have been found to resemble that of the cyanobacteria Synechococcus sp. PCC 6301 and Anabaena sp. PCC 7120. The Synechocystis FOF1 ATP-synthase has nine subunits. A tenth open reading frame with unknown function was detected at the 5′ end of atp1, coding for a putative gene product similar to uncI in Escherichia coli. A promoter structure was inferred for the Synechocystis atp operons and compared to other known promoters of cyanobacteria. Even though the operon structure of atp1 and atp2 in Synechocystis resembles the corresponding operons of Synechococcus, the amino acid sequences of individual gene products show marked differences. Genetic distances between cyanobacterial genes and genes for ATP-synthase subunits from other species have been calculated and compiled into evolutionary trees.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00037050
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  • 4
    Electronic Resource
    Electronic Resource
    Obituary (1992)
    Springer
    Photosynthesis research 31 (1992), S. 165-166 
    Details
    ISSN: 1573-5079
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00035535
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  • 5
    Electronic Resource
    Electronic Resource
    A transcription unit for the Rieske FeS-protein and cytochrome b in Chlorobium limicola (1994)
    Springer
    Photosynthesis research 39 (1994), S. 163-174 
    Details
    ISSN: 1573-5079
    Keywords: cytochrome bc-complex ; electron transport ; Green S-bacteria ; membrane proteins ; petB ; petC
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A transcription unit petCB from Chlorobium limicola is described. The leading gene petC codes for a Rieske FeS-protein of 19.04 kDa with 181 amino acid residues. The following gene petB codes for a cytochrome b of 47.48 kDa with 428 amino acid residues. The transcription unit lacks a third gene pet-A for cytochrome c 1 or-f, which is found in the fbc-operons of gram-negative bacteria. In the derived amino acid sequence for the Rieske FeS-protein the four cysteines and the 2 histidines are conserved in the peptides binding the 2Fe2S-cluster, although the redox potential of the cluster is about 150 mV more negative in Chlorobium. The gene for cytochrome b includes the coding region for an N-terminal, positively charged extension which is typical for Chlorobium. The gene is not split into two parts for cytochrome b 6 and subunit IV. However, a fourteenth amino acid between the two histidines in the fourth, putative transmembrane helix, and the lack of an eighth transmembrane helix at the C-terminus, among other features, clearly resemble the cytochrome b 6 f-complexes. Therefore, the separation into b 6 f- and bc 1-type complexes during evolution must have occurred before the split of the gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00029383
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  • 6
    Electronic Resource
    Electronic Resource
    Identification of the subunit carrying FeS-centers A and B in the P840-reaction center preparation of Chlorobium limicola (1993)
    Springer
    Photosynthesis research 38 (1993), S. 111-114 
    Details
    ISSN: 1573-5079
    Keywords: green sulfur bacteria ; psa-C ; FeS-centers A and B ; bound ferredoxin ; Photosystem 1 reaction center
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The product of the second gene in a transcription unit for the P840-reaction center of Chlorobium limicola f.sp. thiosulfatophilum, which codes for a protein of 23.87 kDa with 232 amino acids, was identified as the subunit migrating in SDS-PAGE at the apparent molecular weight of 32 kDa in reaction center preparations, by Western blotting and N-terminal sequencing. This protein corresponds to PsaC, a 8 kDa-subunit of Photosystem 1 which carries the FeS-centers A and B.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00015067
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  • 7
    Electronic Resource
    Electronic Resource
    Structural conservation and functional diversity of V-ATPases (1992)
    Springer
    Journal of bioenergetics and biomembranes 24 (1992), S. 407-414 
    Details
    ISSN: 1573-6881
    Keywords: Proton pumps ; ATPase ; V-ATPase ; vacuolar system ; eukaryotes ; chromaffin granules ; yeast cells ; mutants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The vacuolar system of eukaryotic cells contains a large number of organelles that are primary energized by an H+-ATPase that was named V-ATPase. The structure and function of V-ATPases from various sources was extensively studied in the last few years. Several genes encoding subunits of the enzyme were cloned and sequenced. The sequence information revealed the relations between V-ATPases and F-ATPases that evolved from common ancestral genes. The two families of proton pumps share structural and functional similarity. They contain distinct peripheral catalytic sectors and hydrophobic membrane sectors. Genes encoding subunits of V-ATPase in yeast cells were interrupted to yield mutants that are devoid of the enzyme and are sensitive to pH and calcium concentrations in the medium. The mutants were used to study structure, function, molecular biology, and biogenesis of the V-ATPase. They also shed light on the functional assembly of the enzyme in the vacuolar system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00762533
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