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  • 1
    Electronic Resource
    Electronic Resource
    Determination of Dimethyl Sulfoxide in Aqueous Solution by an Enzyme-Linked Method (1994)
    s.l. : American Chemical Society
    Analytical chemistry 66 (1994), S. 4093-4096 
    Details
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ac00094a036
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Changes in gross protein and lipid requirements of rainbow trout, Oncorhynchus my kiss (Walbaum), at elevated temperatures (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Aquaculture research 23 (1992), S. 0 
    Details
    ISSN: 1365-2109
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract. In southern Africa rainbow trout, Oncorhynchus my kiss (Walbaum), are generally cultured at temperatures between 18 and 22°C, which is higher than the optimal thermal range for maximum growth in this species. Experiments were undertaken on two size classes of fish (〈4·5g and 〉25g) to determine the gross changes in protein and lipid requirements at these temperatures. The optimal protein and lipid requirements of the smaller fish were found to be 40% and 20–30% of the diet respectively. These levels are significantly different to those under optimal thermal conditions. The protein requirements of the larger fish remained at the ‘threshold level’ of 35% of the diet, although lipid requirements rose lo between 20 and 23% of the diet. The results are discussed in terms of the animal's scope for growth.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2109.1992.tb00604.x
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  • 3
    Electronic Resource
    Electronic Resource
    Preliminary crystallographic studies of dimethylsulfoxide reductase from Rhodobacter capsulatus (1996)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 52 (1996), S. 194-196 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Dimethylsulfoxide reductase from the photosynthetic bacterium Rhodobacter capsulatus has been crystallized in two similar forms which are suitable for X-ray structure determination. Both crystals forms belong to space group P4122 or P4322, with cell dimensions a = b = 80.81, c = 229.75 Å (type I crystals) or a = b = 89.30, c = 230.05 Å (type II crystals) and one molecule in the asymmetric unit. Diffraction has been observed to at least 2.0 Å in type I crystals and to 2.6 Å in type II crystals. Dimethylsulfoxide reductase from Rhodobacter is the simplest molybdenum oxotransferase known and this makes it an ideal model to study the structure and function of this class of enzymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444995007712
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  • 4
    Electronic Resource
    Electronic Resource
    The periplasmic nitrate reductase of Rhodobacter capsulatus; purification, characterisation and distinction from a single reductase for trimethylamine-N-oxide, dimethylsulphoxide and chlorate (1987)
    Springer
    Archives of microbiology 147 (1987), S. 340-345 
    Details
    ISSN: 1432-072X
    Keywords: Rhodobacter capsulatus ; Periplasmic enzymes ; Nitrate reductase ; Trimethylamine-N-oxide/dimethylsulphoxide/chlorate reductase ; Molybdenum cofactor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The periplasmic dissimilatory nitrate reductase from Rhodobacter capsulatus N22DNAR+ has been purified. It comprises a single type of polypeptide chain with subunit molecular weight 90,000 and does not contain heme. Chlorate is not an alternative substrate. A molybdenum cofactor, of the pterin type found in both nitrate reductases and molybdoenzymes from various sources, is present in nitrate reductase from R. capsulatus at an approximate stoichiometry of 1 molecule per polypeptide chain. This is the first report of the occurrence of the cofactor in a periplasmic enzyme. Trimethylamine-N-oxide reductase activity was fractionated by ion exchange chromatography of periplasmic proteins. The fractionated material was active towards dimethylsulphoxide, chlorate and methionine sulphoxide, but not nitrate. A catalytic polypeptide of molecular weight 46,000 was identified by staining for trimethylamine-N-oxide reductase activity after polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate. The same polypeptide also stained for dimethylsulphoxide reductase activity which indicates that trimethylamine-N-oxide and dimethylsulphoxide share a common reductase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00406130
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  • 5
    Electronic Resource
    Electronic Resource
    Identification of a periplasmic dimethylsulphoxide reductase in Hyphomicrobium EG grown under chemolithoheterotrophic conditions with dimethylsulphoxide as carbon source (1994)
    Springer
    Archives of microbiology 162 (1994), S. 148-150 
    Details
    ISSN: 1432-072X
    Keywords: Key words     Hyphomicrobium ; Dimethylsulphoxide reductase ; Periplasmic enzymes ; Chemolithoheterotrophic growth
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract      Hyphomicrobium EG can grow with dimethylsulphoxide as sole carbon and energy source with oxygen as electron acceptor. In the present work we have found that the dimethylsulphoxide reductase of this bacterium could be assayed with dithionite-reduced methylviologen as reductant but not with NADH. Sub-cellular fractionation of Hyphomicrobium EG showed that the dimethylsulphoxide reductase was a periplasmic enzyme. An antibody to the dimethylsulphoxide reductase of Rhodobacter capsulatus cross-reacted with a polypeptide in the periplasmic fraction from Hyphomicrobium EG which had the same M r as the dimethylsulphoxide reductase of Rhodobacter capsulatus. It is suggested that the reduction of dimethylsulphoxide in Hyphomicrobium involves respiratory electron transfer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050117
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  • 6
    Electronic Resource
    Electronic Resource
    Molybdenum active centre of DMSO reductase from Rhodobacter capsulatus: crystal structure of the oxidised enzyme at 1.82-Å resolution and the dithionite-reduced enzyme at 2.8-Å resolution (1997)
    Springer
    JBIC 2 (1997), S. 690-701 
    Details
    ISSN: 1432-1327
    Keywords: Key words DMSO reductase ; Molybdenum ; Pterin ; Molybdopterin ; Crystal structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract  The 1.82-Å X-ray crystal structure of the oxidised (Mo(VI)) form of the enzyme dimethylsulfoxide reductase (DMSOR) isolated from Rhodobacter capsulatus is presented. The structure has been determined by building a partial model into a multiple isomorphous replacement map and fitting the crystal structure of DMSOR from Rhodobacter sphaeroides to the partial model. The enzyme structure has been refined, at 1.82-Å resolution, to an R factor of 14.8% (R free = 18.4%). The molybdenum is coordinated by seven ligands: four dithiolene sulfurs, Oγ of Ser147 and two oxo groups. The four sulfur ligands, at a metal-sulfur distance of 2.4 Å or 2.5 Å, are contributed by the two molybdopterin guanine dinucleotide (MGD) cofactors. The coordination sphere of the molybdenum is different from that in previously reported structures of DMSOR from R. sphaeroides and R. capsulatus. The 2.8-Å structure of DMSOR, reduced by addition of sodium dithionite, is also described and differs from the structure of the oxidised enzyme by the removal of a single oxo ligand from the molybdenum coordination sphere. A structure, at 2.5-Å resolution, has also been obtained from crystals soaked in mother liquor buffered at pH 7.0. No differences are observed in the structure at pH 7 when compared with the native crystal structure at pH 5.5.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007750050185
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  • 7
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    A Role for Lactate Dehydrogenases in the Survival of Neisseria gonorrhoeae in Human Polymorphonuclear Leukocytes and Cervical Epithelial Cells (2014)
    Oxford University Press
    Details
    Publication Date: 2014-09-27
    Description: Lactate is an abundant metabolite, produced by host tissues and commensal organisms, and it represents an important potential carbon source for bacterial pathogens. In the case of Neisseria spp., the importance of the lactate permease in colonization of the host has been demonstrated, but there have been few studies of lactate metabolism in pathogenic Neisseria in the postgenomic era. We describe herein the characterization of genome-annotated, respiratory, and substrate-level lactate dehydrogenases (LDHs) from the obligate human pathogen Neisseria gonorrhoeae . Biochemical assays using N. gonorrhoeae 1291 wild type and isogenic mutant strains showed that cytoplasmic LdhA (NAD + -dependent D -lactate dehydrogenase) and the membrane-bound respiratory enzymes, LdhD ( D -lactate dehydrogenase) and LldD ( L -lactate dehydrogenase) are correctly annotated. Mutants lacking LdhA and LdhD showed greatly reduced survival in neutrophils compared with wild type cells, highlighting the importance of D -lactate metabolism in gonococcal survival. Furthermore, an assay of host colonization using the well-established human primary cervical epithelial cell model revealed that the two respiratory enzymes make a significant contribution to colonization of and survival within the microaerobic environment of the host. Taken together, these data suggest that host-derived lactate is critical for the growth and survival of N. gonorrhoeae in human cells.
    Print ISSN: 0022-1899
    Electronic ISSN: 1537-6613
    Topics: Medicine
    Published by Oxford University Press on behalf of The Infectious Diseases Society of America (IDSA).
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  • 8
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    Copper(II)-Bis(Thiosemicarbazonato) Complexes as Antibacterial Agents: Insights into Their Mode of Action and Potential as Therapeutics [Mechanisms of Action] (2015)
    The American Society for Microbiology (ASM)
    Details
    Publication Date: 2015-09-19
    Description: There is increasing interest in the use of lipophilic copper (Cu)-containing complexes to combat bacterial infections. In this work, we showed that Cu complexes with bis(thiosemicarbazone) ligands [Cu(btsc)] exert antibacterial activity against a range of medically significant pathogens. Previous work using Neisseria gonorrhoeae showed that Cu(btsc) complexes may act as inhibitors of respiratory dehydrogenases in the electron transport chain. We now show that these complexes are also toxic against pathogens that lack a respiratory chain. Respiration in Escherichia coli was slightly affected by Cu(btsc) complexes, but our results indicate that, in this model bacterium, the complexes act primarily as agents that deliver toxic Cu ions efficiently into the cytoplasm. Although the chemistry of Cu(btsc) complexes may dictate their mechanism of action, their efficacy depends heavily on bacterial physiology. This is linked to the ability of the target bacterium to tolerate Cu and, additionally, the susceptibility of the respiratory chain to direct inhibition by Cu(btsc) complexes. The physiology of N. gonorrhoeae , including multidrug-resistant strains, makes it highly susceptible to damage by Cu ions and Cu(btsc) complexes, highlighting the potential of Cu(btsc) complexes (and Cu-based therapeutics) as a promising treatment against this important bacterial pathogen.
    Print ISSN: 0066-4804
    Electronic ISSN: 1098-6596
    Topics: Biology , Medicine
    Published by The American Society for Microbiology (ASM)
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  • 9
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    A genetic screen reveals a periplasmic copper chaperone required for nitrite reductase activity in pathogenic Neisseria [Research Communication] (2015)
    The Federation of American Societies for Experimental Biology (FASEB)
    Details
    Publication Date: 2015-09-02
    Description: Under conditions of low oxygen availability, Neisseria meningitidis and Neisseria gonorrhoeae are able to respire via a partial denitrification pathway in which nitrite is converted to nitrous oxide. In this process, nitrite reductase (AniA), a copper (Cu)-containing protein converts nitrite to NO, and this product is converted to nitrous oxide by nitric oxide reductase (NorB). NorB also confers protection against toxic NO, and so we devised a conditional lethal screen, using a norB mutant, to identify mutants that were resistant to nitrite-dependent killing. After random-deletion mutagenesis of N. meningitidis , this genetic screen identified a gene encoding a Cu chaperone that is essential for AniA function, AccA. Purified AccA binds one Cu (I) ion and also possesses a second binding site for Cu (II). This novel periplasmic Cu chaperone (AccA) appears to be essential for provision of Cu ions to AniA of pathogenic Neisseria to generate an active nitrite reductase. Apart from the Neisseria genus, AccA is distributed across a wide range of environmental Proteobacteria species.—Jen, F. E.-C., Djoko, K. Y., Bent, S. J., Day, C. J., McEwan, A. G., Jennings, M. P. A genetic screen reveals a periplasmic copper chaperone required for nitrite reductase activity in pathogenic Neisseria .
    Print ISSN: 0892-6638
    Electronic ISSN: 1530-6860
    Topics: Biology
    Published by The Federation of American Societies for Experimental Biology (FASEB)
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  • 10
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    MINIREVIEW: Copper and Zinc against Bacterial Pathogens [Molecular Bases of Disease] (2015)
    The American Society for Biochemistry and Molecular Biology (ASBMB)
    Details
    Publication Date: 2015-08-01
    Description: Zinc (Zn) and copper (Cu) are essential for optimal innate immune function, and nutritional deficiency in either metal leads to increased susceptibility to bacterial infection. Recently, the decreased survival of bacterial pathogens with impaired Cu and/or Zn detoxification systems in phagocytes and animal models of infection has been reported. Consequently, a model has emerged in which the host utilizes Cu and/or Zn intoxication to reduce the intracellular survival of pathogens. This review describes and assesses the potential role for Cu and Zn intoxication in innate immune function and their direct bactericidal function.
    Print ISSN: 0021-9258
    Electronic ISSN: 1083-351X
    Topics: Biology , Chemistry and Pharmacology
    Published by The American Society for Biochemistry and Molecular Biology (ASBMB)
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