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  • 1
    Electronic Resource
    Electronic Resource
    EXAFS investigation of the active site of iron superoxide dismutase of Escherichia coli and Propionibacterium shermanii (1996)
    Springer
    European biophysics journal 24 (1996), S. 243-250 
    Details
    ISSN: 1432-1017
    Keywords: Iron superoxide dismutase ; SOD ; X-ray absorption ; XAS ; Extended X-ray absorption fine structure ; EXAFS ; P. shermanii ; E. coli ; Metalloproteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract The local structure of the iron site in ferric superoxide dismutase from P. shermanii was analyzed by X-ray absorption spectroscopy. The metal-ligand cluster of the enzyme is found to be similar to the crystallographically investigated ferric superoxide dismutase from E. coli. At pH 6.4 the enzyme is five-fold coordinated with three histidines, an aspartate and a water molecule. The average bond lengths between the metal and the histidines are about 2.10 Å, between metal and aspartate they are about 1.86 Å and between metal and water 1.96 Å. With an increase in pH a change in the coordination number from five to six is observed both in pre-edge peak and EXAFS spectra analysis. However, the bond lengths of the ligands do not change dramatically, they are conserved for the aspartate and increase slightly to 2.13 Å for the average metal - histidine distance at pH 9.3. The observation of the increase in coordination number is correlated with a decrease in enzymatic activity which occurs in the high pH range. The zinc EXAFS spectra of P. shermanii superoxide dismutase have shown that zinc can be incorporated in the active center instead of the iron.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00205105
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  • 2
    Electronic Resource
    Electronic Resource
    Identification of Export Proteins from Mycobacterium tuberculosis That Interact with SecA (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 797 (1996), 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.1749-6632.1996.tb52964.x
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  • 3
    Electronic Resource
    Electronic Resource
    Discovery of hardest known oxide (1996)
    [s.l.] : Nature Publishing Group
    Nature 383 (1996), S. 401-401 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] SIR á€" Microhardness measurements on synthesized samples of stishovite, a high-pressure phase of silica, show that it is the hardest oxide yet discovered. Among polycrystalline materials, its hardness (33 gigapascals, GPa) rivals those of the hardest materials. Despite many ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/383401a0
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  • 4
    Electronic Resource
    Electronic Resource
    Electrochemical tuning of the lifetime of the CO stretching vibration for CO/Pt(111) (1996)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 104 (1996), S. 2438-2445 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: We have used the large electric fields at the interface of a Pt(111) electrode and an acetonitrile electrolyte solution to tune the interaction between adsorbed CO and the Pt(111) surface. The electrode potential is varied over a 2.5 Volt range. As the electrode potential is made more positive, the CO vibrational frequency increases and the vibrational lifetime decreases. Over the potential range investigated, the tuning is about 35–40 cm−1 and the lifetime varies from ≈2.1 to ≈1.5 ps. Ab initio calculations performed for CO/Cu(100) predicted the opposite trend for the lifetimes for that system [M. Head-Gordon and J. C. Jully, Chem. Phys. 175, 37 (1993)]. Within an empirical model of nonadiabatic charge transfer [B. N. J. Persson and M. Persson, Solid State Commun. 36, 175 (1980)], our observations can be explained by a decreasing 2π-derived density of states of the Pt/CO complex at the Fermi level. © 1996 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.470938
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  • 5
    Electronic Resource
    Electronic Resource
    Processing of the AIDA-I precursor: removal of AIDAC and evidence for the outer membrane anchoring as a β-barrel structure (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 22 (1996), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The AIDA-I adhesin known to be responsible for the diffuse adherence (DA) phenotype of the diarrhoea-genie Escherichia coli (DAEC) strain 2787 has been shown previously to be synthesized as a precursor protein and to undergo additional C-terminal processing. Here, the C-terminal processing of the AIDA-I precursor and the outer membrane topology of the cleaved C-terminal fragment, AIDAC, were investigated. By isolation of the cleaved AIDAC fragment and N-terminal sequencing, the C-terminal cleavage site was identified between Ser-846 and Ala-847 thereby indicating a molecular mass of 47.5 kDa for AIDAC. The correct processing to AIDA-I and AIDAC in OmpT, OmpP and DegP protease-deficient E. coli strains as well as in avirulent salmonellae and shigellae points to an autocatalytic cleavage mechanism. The cleaved AIDAC was localized in the outer membrane. A leader sequence-AIDAC fusion was efficiently routed to the outer membrane. Analysis by protease digestion, secondary-structure prediction and modelling, by comparison with structurally related bacterial proteins like the lgA1 protease from neisseria, the vacuolating toxin from Helicobacter pylori, and the VirG protein of Shigella flexneri, strongly indicates that AIDAC is present in the outer membrane as a β-barrel structure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1996.tb02653.x
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  • 6
    Electronic Resource
    Electronic Resource
    Processing of antennular input in the brain of the spiny lobster, Panulirus argus (1996)
    Springer
    Journal of comparative physiology 178 (1996), S. 579-604 
    Details
    ISSN: 1432-1351
    Keywords: Crustacean ; Chemoreception ; Mechanoreception ; Deutocerebrum ; Motoneurons ; Projection neurons
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Neurons in the brain of the spiny lobster that respond to chemical and mechanical stimulation of the antennule (antenna I) were recorded and stained intracellularly. Described here are neurons that do not arborize in the olfactory and accessory lobes of the deutocerebrum, but rather primarily target the lateral and/or the median antennular neuropils of the deutocerebrum. Some of the neurons also extend into the antennal and tegumentary neuropils of the tritocerebrum and the neuropils of the median protocerebrum. Included are antennular sensory afferents, antennular motoneurons, projection neurons descending from the central brain, projection neurons ascending from the central brain and projection neurons descending from the eyestalk ganglia. Collectively, these neurons consitutute a novel antennular sensory pathway that is parallel to and independent of the antennular olfactory pathway. The novel pathway integrates mechanosensory and non-olfactory chemosensory information in the lateral and/or the median antennular neuropils, which also serve as lower motor centers of the antennule. Division of the arthropod deutocerebrum into two, functionally distinct chemosensory pathways may reflect differences in how chemosensory information is processed that is fundamental to understanding the origin of the sense of smell.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00227374
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  • 7
    Electronic Resource
    Electronic Resource
    Processing of antennular input in the brain of the spiny lobster, Panulirus argus (1996)
    Springer
    Journal of comparative physiology 178 (1996), S. 605-628 
    Details
    ISSN: 1432-1351
    Keywords: Crustacean ; Olfaction ; Mechanoreception ; Local interneurons ; Projection neurons
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Neurons in the olfactory deutocerebrum of the spiny lobster, Panulirus argus, were recorded intracellularly and filled with biocytin. Recorded neurons arborized in the olfactory lobe (OL), a glomerular neuropil innervated by olfactory and some presumptive mechanosensory antennular afferents. The neurons responded to chemosensory input from the lateral antennular flagellum bearing the olfactory sensilla but not the medial flagellum bearing many non-olfactory chemosensory sensilla. Many neurons received additional mechanosensory input. Thus the OL integrates specifically olfactory with mechanosensory input. OL neurons had multiglomerular arborizations restricted to one or two of the three horizontal layers of the columnar glomeruli. OL local interneurons comprised “core” neurons with tree-like neurites and terminals in the base of the glomeruli and “rim” neurons with neurites surrounding the OL and terminals in the cap/subcap. The somata of OL local interneurons lay in the medial soma cluster (100000 somata). OL projection neurons arborized in the base of the glomeruli and ascended via the olfactory glomerular tract to the lateral protocerebrum. A parallel projection pathway is constituted by projection neurons of the accessory lobe, a glomerular neuropil without afferent innervation but intimate links to the OL. The projection neuron somata constituted the lateral soma cluster (200000 somata).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00227375
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  • 8
    Electronic Resource
    Electronic Resource
    Comparison of the expression of a plastidic chaperonin 60 in different plant tissues and under photosynthetic and non-photosynthetic conditions (1996)
    Springer
    Planta 200 (1996), S. 326-334 
    Details
    ISSN: 1432-2048
    Keywords: Chaperone ; Chloroplasts ; Chromoplasts ; Heat-shock protein ; Secale
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A partial cDNA which codes for the β-subunit of a plastidic chaperonin 60 (cpn60-β) from rye (Secale cereale L.) leaves was identified and sequenced, except for 46 amino acids of the N-terminus of the mature protein and the transit sequence. This is the first cpn60-β sequence determined for a monocotyledonous plant. Specific antibodies against cpn60-β were affinity-purified from an antiserum raised against the total soluble protein fraction of ribosome-deficient plastids. The localization of cpn60-β in chloroplasts or non-green plastids was confirmed by immunodetection in Percoll gradient-purified organelles. The expression and occurrence of cpn60-β was analysed by immunoblotting with the specific antibodies and Northern hybridization. The cpn60-β protein was constitutively expressed in various green and non-green tissues. It was evenly distributed along the major part of a rye leaf, while highest transcript levels occurred in the youngest and oldest leaf sections. The expression of the cpn60-β protein was not enhanced by a heat-shock treatment at 42 °C. The cpn60-β transcript and protein were more strongly expressed in various non-green, for instance etiolated, 70S-ribosome-deficient 32 °C-grown, or herbicide-bleached tissues, than in green leaves of rye. A rapid increase in the cpn60-β transcript level was also observed when green leaves were transferred from light to darkness while the protein level was not affected. The dark-induced increase in the cpn60-β transcript was totally suppressed in the presence of 2% sucrose. Inhibitor treatments suggested that the change in cpn60-β transcript level was not related to changes of the ATP supply of the tissue. While the large subunit of the photosynthetic protein ribulose-1,5-bisphosphate carboxylase was largely degraded during ripening of tomato fruits, high levels of cpn60-β were detected in tomato chromoplasts and in the yellow flower petals of Narcissus. Low levels of cpn60-β were detected in root tissue.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00200300
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  • 9
    Electronic Resource
    Electronic Resource
    Somaclonal variation of the mitochondrial ATPase subunit 6 gene region in regenerated triticale shoots and full-grown plants (1996)
    Springer
    Theoretical and applied genetics 93 (1996), S. 355-360 
    Details
    ISSN: 1432-2242
    Keywords: Somaclonal variation ; Cytoplasmic male sterility ; Triticale ; Regeneration ; Mitochondrial atp6 gene region
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Comparative hybridization analyses of total DNA from fertile and cytoplasmic male-sterile (CMS) triticale plants which had been regenerated from embryogenic callus cultures revealed the organization and variation of the mitochondrial atp6 gene region. In order to compare different developmental phases, we analysed mitochondrial DNA (mtDNA) from both the shoots and full-grown regenerants. Somaclonal variants were identified on the basis of differences in the mtDNA from fertile and CMS triticale. Several shoots as well as all of the full-grown plants analysed showed somaclonal variation. This phenomenon could be traced back to having primarily orginated from the influence of the nuclear background, which give rise to a stoichiometric increase in a rye-specific orf25 gene copy, and a tissue culture-induced combination of fertile and CMS-specific mtDNA organization of the atp6 gene area. The latter event is probably caused by the homologous recombination of repetitive sequences that may be accompanied by selective amplifications.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00223176
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  • 10
    Electronic Resource
    Electronic Resource
    Somaclonal variation of the mitochondrial ATPase subunit 6 gene region in regenerated triticale shoots and full-grown plants (1996)
    Springer
    Theoretical and applied genetics 93 (1996), S. 355-360 
    Details
    ISSN: 1432-2242
    Keywords: Key words Somaclonal variation  ;  Cytoplasmic male sterility  ;  Triticale  ;  Regeneration  ;  Mitochondrial atp6 gene region
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Comparative hybridization analyses of total DNA from fertile and cytoplasmic male-sterile (CMS) triticale plants which had been regenerated from embryogenic callus cultures revealed the organization and variation of the mitochondrial atp6 gene region. In order to compare different developmental phases, we analysed mitochondrial DNA (mtDNA) from both the shoots and full-grown regenerants. Somaclonal variants were identified on the basis of differences in the mtDNA from fertile and CMS triticale. Several shoots as well as all of the full-grown plants analysed showed somaclonal variation. This phenomenon could be traced back to having primarily orginated from the influence of the nuclear background, which give rise to a stoichiometric increase in a rye-specific orf25 gene copy, and a tissue culture-induced combination of fertile and CMS-specific mtDNA organization of the atp6 gene area. The latter event is probably caused by the homologous recombination of repetitive sequences that may be accompanied by selective amplifications.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001220050288
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