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  • 1
    Online Resource
    Online Resource
    Preparation, physicochemical characterization and biological evaluation of cefodizime metal ion complexes
    Oxford University Press (OUP) ; 2010
    In:  Journal of Pharmacy and Pharmacology Vol. 61, No. 6 ( 2010-01-08), p. 753-758
    Details
    In: Journal of Pharmacy and Pharmacology, Oxford University Press (OUP), Vol. 61, No. 6 ( 2010-01-08), p. 753-758
    Abstract: Cefodizime is a broad spectrum cephalosporin belonging to the third generation agents. In this study, attention has been paid to the preparation, physicochemical characterization and biological evaluation of new Cu2+, Zn2+, Fe3+, Co2+ and Al3+ complexes of cefodizime. Methods The stoichiometrics and the mode of bonding of the complexes were deduced from their elemental and metal analysis, electrical conductivity measurements, UV-vis, infrared and Raman spectroscopic investigations. Study of the stoichiometry of these complexes referred to the formation of 1: 1 ratios of metal to ligand. Antimicrobial activity of the complexes was determined using two strains of Gram-positive (Bacillus subtilis and Proteus vulgaris) and two strains of Gram-negative (Escherichia coli W3110 and Pseudomonas putida) bacteria. The minimal inhibitory concentration was determined as the lowest concentration inhibiting bacterial growth on solid Luria Bertani medium. Key findings The spectra gave evidence as to the position of binding. In addition, the aqueous solubility of cefodizime was strongly reduced by complexation. Conclusions The antibacterial activity of cefodizime was not affected by complexation with Al3+ but it was reduced by complexation with the other tested metal ions against the bacteria under study.
    Type of Medium: Online Resource
    ISSN: 0022-3573 , 2042-7158
    URL: Article
    DOI: 10.1211/jpp.61.06.0007
    Language: English
    Publisher: Oxford University Press (OUP)
    Publication Date: 2010
    detail.hit.zdb_id: 2041988-0
    detail.hit.zdb_id: 2050532-2
    SSG: 15,3
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  • 2
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    Online Resource
    Survival of Escherichia coli Cells on Solid Copper Surfaces Is Increased by Glutathione
    American Society for Microbiology ; 2014
    In:  Applied and Environmental Microbiology Vol. 80, No. 22 ( 2014-11-15), p. 7071-7078
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 80, No. 22 ( 2014-11-15), p. 7071-7078
    Abstract: Bacteria are rapidly killed on solid copper surfaces, so this material could be useful to limit the spread of multiple-drug-resistant bacteria in hospitals. In Escherichia coli , the DNA-protecting Dps protein and the NADH:ubiquinone oxidoreductase II Ndh were not involved in tolerance to copper ions or survival on solid copper surfaces. Decreased copper tolerance under anaerobic growth conditions in the presence of ascorbate and with melibiose as the carbon source indicated that sodium-dependent symport systems may provide an import route for Cu I into the cytoplasm. Glutathione-free Δ copA Δ gshA double mutants of E. coli were more rapidly inactivated on solid copper surfaces than glutathione-containing wild-type cells. Therefore, while DNA protection by Dps was not required, glutathione was needed to protect the cytoplasm and the DNA against damage mediated by solid copper surfaces, which may explain the differences in the molecular mechanisms of killing between glutathione-containing Gram-negative and glutathione-free Gram-positive bacteria.
    Type of Medium: Online Resource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/AEM.02842-14
    RVK:
    WA 15000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2014
    detail.hit.zdb_id: 223011-2
    detail.hit.zdb_id: 1478346-0
    SSG: 12
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  • 3
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    Online Resource
    Genomic Analyses of Transport Proteins in Ralstonia metallidurans
    Hindawi Limited ; 2005
    In:  Comparative and Functional Genomics Vol. 6, No. 1-2 ( 2005), p. 17-56
    Details
    In: Comparative and Functional Genomics, Hindawi Limited, Vol. 6, No. 1-2 ( 2005), p. 17-56
    Abstract: Ralstonia (Wautersia, Cupriavidus) metallidurans (Rme) is better able to withstand high concentrations of heavy metals than any other well-studied organism. This fact renders it a potential agent of bioremediation as well as an ideal model organism for understanding metal resistance phenotypes. We have analysed the genome of Rme for genes encoding homologues of established and putative transport proteins; 13% of all genes in Rme encode such homologues. Nearly one-third of the transporters identified (32%) appear to function in inorganic ion transport with three-quarters of these acting on cations. Transporters specific for amino acids outnumber sugar transporters nearly 3: 1, and this fact plus the large number of uptake systems for organic acids indicates the heterotrophic preferences of these bacteria. Putative drug efflux pumps comprise 10% of the encoded transporters, but numerous efflux pumps for heavy metals, metabolites and macromolecules were also identified. The results presented should facilitate genetic manipulation and mechanistic studies of transport in this remarkable bacterium.
    Type of Medium: Online Resource
    ISSN: 1531-6912 , 1532-6268
    URL: Article
    DOI: 10.1002/cfg.454
    Language: English
    Publisher: Hindawi Limited
    Publication Date: 2005
    detail.hit.zdb_id: 2054345-1
    detail.hit.zdb_id: 2711883-6
    SSG: 12
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  • 4
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    Online Resource
    New genes involved in chromate resistance in Ralstonia metallidurans strain CH34
    Springer Science and Business Media LLC ; 2004
    In:  Archives of Microbiology Vol. 181, No. 5 ( 2004-5-1), p. 390-390
    Details
    In: Archives of Microbiology, Springer Science and Business Media LLC, Vol. 181, No. 5 ( 2004-5-1), p. 390-390
    Type of Medium: Online Resource
    ISSN: 0302-8933 , 1432-072X
    URL: Article
    DOI: 10.1007/s00203-004-0665-5
    RVK:
    WA 15000
    Language: Unknown
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2004
    detail.hit.zdb_id: 1458451-7
    detail.hit.zdb_id: 477-7
    detail.hit.zdb_id: 124824-8
    SSG: 12
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  • 5
    Online Resource
    Online Resource
    CHR, a Novel Family of Prokaryotic Proton Motive Force-Driven Transporters Probably Containing Chromate/Sulfate Antiporters
    American Society for Microbiology ; 1998
    In:  Journal of Bacteriology Vol. 180, No. 21 ( 1998-11), p. 5799-5802
    Details
    In: Journal of Bacteriology, American Society for Microbiology, Vol. 180, No. 21 ( 1998-11), p. 5799-5802
    Abstract: We describe a small family of proteins, CHR, which contains members that function in chromate and/or sulfate transport. CHR proteins occur in bacteria and archaea. They consist of about 400 amino acyl residues, appear to have 10 transmembrane α-helical segments in an unusual 4+6 arrangement, and arose by an intragenic duplication event.
    Type of Medium: Online Resource
    ISSN: 0021-9193 , 1098-5530
    URL: Article
    DOI: 10.1128/JB.180.21.5799-5802.1998
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1998
    detail.hit.zdb_id: 1481988-0
    SSG: 12
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  • 6
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    Online Resource
    High-Level Resistance to Cobalt and Nickel but Probably No Transenvelope Efflux: Metal Resistance in the Cuban Serratia marcescens Strain C-1
    Springer Science and Business Media LLC ; 2007
    In:  Microbial Ecology Vol. 53, No. 1 ( 2007-1-29), p. 123-133
    Details
    In: Microbial Ecology, Springer Science and Business Media LLC, Vol. 53, No. 1 ( 2007-1-29), p. 123-133
    Type of Medium: Online Resource
    ISSN: 0095-3628 , 1432-184X
    URL: Article
    DOI: 10.1007/s00248-006-9152-7
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2007
    detail.hit.zdb_id: 1462065-0
    detail.hit.zdb_id: 188257-0
    SSG: 12
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  • 7
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    Online Resource
    Alcaligenes eutrophus as a Bacterial Chromate Sensor
    American Society for Microbiology ; 1998
    In:  Applied and Environmental Microbiology Vol. 64, No. 2 ( 1998-02), p. 453-458
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 64, No. 2 ( 1998-02), p. 453-458
    Abstract: In Alcaligenes eutrophus CH34, determinants encoding inducible resistance to chromate ( chr ) and to cobalt and nickel ( cnr ) are located adjacent to each other on plasmid pMOL28. To develop metal-sensing bacterial strains, a cloned part of plasmid pMOL28, which contains both determinants, was mutated with Tn 5-lacZ . The chr :: lacZ fusions were specifically induced by chromium; cnr was induced best by Ni 2+ but was also induced by Co 2+ , Mn 2+ , chromate, Cu 2+ , Cd 2+ , and Zn 2+ . The broad-host-range IncP1 plasmid pEBZ141, which contains a chr :: lux fusion, was constructed. A. eutrophus AE104(pEBZ141), carrying a chr :: lux transcriptional fusion, could be used as a biosensor for chromate when cultivated in glycerol as an optimal carbon source. Chromate and bichromate were the best inducers; induction by Cr 3+ was 10 times lower, and other ions induced only a little or not at all. Interactions among induction of the chr resistance determinant, chromate reduction, chromate accumulation, and the sulfate concentration of the growth medium were demonstrated.
    Type of Medium: Online Resource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/AEM.64.2.453-458.1998
    RVK:
    WA 15000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1998
    detail.hit.zdb_id: 223011-2
    detail.hit.zdb_id: 1478346-0
    SSG: 12
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  • 8
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    Online Resource
    Efflux-mediated heavy metal resistance in prokaryotes
    Oxford University Press (OUP) ; 2003
    In:  FEMS Microbiology Reviews Vol. 27, No. 2-3 ( 2003-06), p. 313-339
    Details
    In: FEMS Microbiology Reviews, Oxford University Press (OUP), Vol. 27, No. 2-3 ( 2003-06), p. 313-339
    Type of Medium: Online Resource
    ISSN: 1574-6976
    URL: Article
    DOI: 10.1016/S0168-6445(03)00048-2
    Language: English
    Publisher: Oxford University Press (OUP)
    Publication Date: 2003
    detail.hit.zdb_id: 1500468-5
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  • 9
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    Online Resource
    Transition Metal Homeostasis
    American Society for Microbiology ; 2009
    In:  EcoSal Plus Vol. 3, No. 2 ( 2009-02-13)
    Details
    In: EcoSal Plus, American Society for Microbiology, Vol. 3, No. 2 ( 2009-02-13)
    Abstract: This chapter focuses on transition metals. All transition metal cations are toxic—those that are essential for Escherichia coli and belong to the first transition period of the periodic system of the element and also the "toxic-only" metals with higher atomic numbers. Common themes are visible in the metabolism of these ions. First, there is transport. High-rate but low-affinity uptake systems provide a variety of cations and anions to the cells. Control of the respective systems seems to be mainly through regulation of transport activity (flux control), with control of gene expression playing only a minor role. If these systems do not provide sufficient amounts of a needed ion to the cell, genes for ATP-hydrolyzing high-affinity but low-rate uptake systems are induced, e.g., ABC transport systems or P-type ATPases. On the other hand, if the amount of an ion is in surplus, genes for efflux systems are induced. By combining different kinds of uptake and efflux systems with regulation at the levels of gene expression and transport activity, the concentration of a single ion in the cytoplasm and the composition of the cellular ion "bouquet" can be rapidly adjusted and carefully controlled. The toxicity threshold of an ion is defined by its ability to produce radicals (copper, iron, chromate), to bind to sulfide and thiol groups (copper, zinc, all cations of the second and third transition period), or to interfere with the metabolism of other ions. Iron poses an exceptional metabolic problem due its metabolic importance and the low solubility of Fe(III) compounds, combined with the ability to cause dangerous Fenton reactions. This dilemma for the cells led to the evolution of sophisticated multi-channel iron uptake and storage pathways to prevent the occurrence of unbound iron in the cytoplasm. Toxic metals like Cd 2+ bind to thiols and sulfide, preventing assembly of iron complexes and releasing the metal from iron-sulfur clusters. In the unique case of mercury, the cation can be reduced to the volatile metallic form. Interference of nickel and cobalt with iron is prevented by the low abundance of these metals in the cytoplasm and their sequestration by metal chaperones, in the case of nickel, or by B 12 and its derivatives, in the case of cobalt. The most dangerous metal, copper, catalyzes Fenton-like reactions, binds to thiol groups, and interferes with iron metabolism. E. coli solves this problem probably by preventing copper uptake, combined with rapid efflux if the metal happens to enter the cytoplasm.
    Type of Medium: Online Resource
    ISSN: 2324-6200
    URL: Article
    DOI: 10.1128/ecosalplus.5.4.4.3
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2009
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  • 10
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    Online Resource
    The ancient alarmone ZTP and zinc homeostasis in Bacillus subtilis
    Wiley ; 2019
    In:  Molecular Microbiology Vol. 112, No. 3 ( 2019-09), p. 741-746
    Details
    In: Molecular Microbiology, Wiley, Vol. 112, No. 3 ( 2019-09), p. 741-746
    Abstract: In Bacillus subtilis a sophisticated regulatory circuit that involves Z nucleoside triphosphate (ZTP) is recruited to optimize cellular zinc distribution when cytoplasmic zinc is scarce. This process uses enzymatic reactions to measure the pool of available zinc ions and amplifies this signal to control the activity of zinc chaperones. The ZTP‐dependent regulatory circuit that is exploited for zinc homeostasis controls purine and folate biosynthesis, which starts with GTP as initial substrate. Low concentrations of formyl‐tetrahydrofolate (fTHF) lead to accumulation of the intermediate 5′‐phosphoribosyl‐4‐carboxyamide‐5‐aminoimidazole (AICAR or ZMP), which is pyrophosphorylated by another intermediate to ZTP. This alarmone activates expression of genes using a ZTP‐dependent riboswitch in many bacterial strains. In this way, the cellular folate concentration controls folate biosynthesis via the enzymatic activity of the fTHF‐dependent AICAR‐transforming reaction. Zinc distribution control is layered onto this circuit. The ‘sensor’ is the activity of the initial reaction of folate synthesis from GTP, which is catalyzed by a zinc‐dependent enzyme FolE IA or its metal‐cambialistic paralog FolE IB . Consequently, low zinc lowers folate levels, causing AICAR accumulation and ZTP formation. In addition to the riboswitch, ZTP activates the zinc chaperone ZagA of the COG0523 protein family, which efficiently allocate zinc to zinc‐dependent enzymes such as FolE IA .
    Type of Medium: Online Resource
    ISSN: 0950-382X , 1365-2958
    URL: Issue
    URL: Article
    DOI: 10.1111/mmi.v112.3
    DOI: 10.1111/mmi.14332
    Language: English
    Publisher: Wiley
    Publication Date: 2019
    detail.hit.zdb_id: 1501537-3
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