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Article ; Online: The Role of the Nucleotides in the Insertion of the bis-Molybdopterin Guanine Dinucleotide Cofactor into apo-Molybdoenzymes.

Tiedemann, Kim / Iobbi-Nivol, Chantal / Leimkühler, Silke

2022 Volume 27, Issue 9

Abstract: The role of the GMP nucleotides of the bis-molybdopterin guanine dinucleotide (bis-MGD) cofactor of the DMSO reductase family has long been a subject of discussion. The recent characterization of the bis-molybdopterin (bis-Mo-MPT) cofactor present in ... ...

Abstract	The role of the GMP nucleotides of the bis-molybdopterin guanine dinucleotide (bis-MGD) cofactor of the DMSO reductase family has long been a subject of discussion. The recent characterization of the bis-molybdopterin (bis-Mo-MPT) cofactor present in the
MeSH term(s)	Coenzymes/metabolism ; Escherichia coli/metabolism ; Guanine Nucleotides/metabolism ; Metalloproteins/metabolism ; Molybdenum/metabolism ; Nucleotides/metabolism ; Pterins
Chemical Substances	Coenzymes ; Guanine Nucleotides ; Metalloproteins ; Nucleotides ; Pterins ; molybdopterin guanine dinucleotide (128007-95-4) ; Molybdenum (81AH48963U)
Language	English
Publishing date	2022-05-06
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	1413402-0
ISSN	1420-3049 ; 1431-5165 ; 1420-3049
ISSN (online)	1420-3049
ISSN	1431-5165 ; 1420-3049
DOI	10.3390/molecules27092993
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Article ; Online: The Shewanella genus: ubiquitous organisms sustaining and preserving aquatic ecosystems.

Lemaire, Olivier N / Méjean, Vincent / Iobbi-Nivol, Chantal

FEMS microbiology reviews

2020 Volume 44, Issue 2, Page(s) 155–170

Abstract: The Gram-negative Shewanella bacterial genus currently includes about 70 species of mostly aquatic γ--proteobacteria, which were isolated around the globe in a multitude of environments such as surface freshwater and the deepest marine trenches. Their ... ...

Abstract	The Gram-negative Shewanella bacterial genus currently includes about 70 species of mostly aquatic γ--proteobacteria, which were isolated around the globe in a multitude of environments such as surface freshwater and the deepest marine trenches. Their survival in such a wide range of ecological niches is due to their impressive physiological and respiratory versatility. Some strains are among the organisms with the highest number of respiratory systems, depending on a complex and rich metabolic network. Implicated in the recycling of organic and inorganic matter, they are important components of organism-rich oxic/anoxic interfaces, but they also belong to the microflora of a broad group of eukaryotes from metazoans to green algae. Examples of long-term biological interactions like mutualism or pathogeny have been described, although molecular determinants of such symbioses are still poorly understood. Some of these bacteria are key organisms for various biotechnological applications, especially the bioremediation of hydrocarbons and metallic pollutants. The natural ability of these prokaryotes to thrive and detoxify deleterious compounds explains their use in wastewater treatment, their use in energy generation by microbial fuel cells and their importance for resilience of aquatic ecosystems.
MeSH term(s)	Aquatic Organisms/physiology ; Ecosystem ; Environmental Microbiology ; Industrial Microbiology ; Shewanella/classification ; Shewanella/physiology ; Symbiosis
Language	English
Publishing date	2020-01-22
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	283740-7
ISSN	1574-6976 ; 0168-6445
ISSN (online)	1574-6976
ISSN	0168-6445
DOI	10.1093/femsre/fuz031
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Article: The Tol-Pal system of Escherichia coli plays an unexpected role in the import of the oxyanions chromate and phosphate

Chaouche, Amine Ali / Houot, Laetitia / Duché, Denis / Iobbi-Nivol, Chantal / Giudici-Orticoni, Marie-Thérèse / Fons, Michel / Méjean, Vincent

Research in microbiology. 2022 May 24,

2022

Abstract: Chromate is a toxic metal that enters bacteria by using oxyanion importers. Here, we show that each mutant of the Tol-Pal system of Escherichia coli exhibited increased chromate resistance. This system, which spans the cell envelope, plays a major role ... ...

Abstract	Chromate is a toxic metal that enters bacteria by using oxyanion importers. Here, we show that each mutant of the Tol-Pal system of Escherichia coli exhibited increased chromate resistance. This system, which spans the cell envelope, plays a major role in envelope integrity and septation. The ΔtolQR mutant accumulated three-fold less chromate than the wild-type. Addition of phosphate but not sulfate to rich medium drastically reduced chromate toxicity and import in the wild-type strain. Furthermore, the intracellular concentration of free inorganic phosphate was significantly reduced for the ΔtolR mutant in comparison to the wild-type strain. Moreover, extracellular labelled phosphate was significantly less incorporated into the ΔtolR mutant. Finally, two distinct TolQR mutant complexes, specifically affected in Tol-Pal energization without affecting the TolQRA complex structure, did not complement the ΔtolQR mutant for inorganic phosphate accumulation. We thus propose that, while the Pst system is well known to import inorganic phosphate, the Tol-Pal system participates to phosphate uptake in particular at medium to high extracellular phosphate concentrations. Since mutations disabling the Tol-Pal system lead to pleiotropic effects, chromate resistance and reduced inorganic phosphate import could occur from an indirect effect of mutations in components of the Tol-Pal system.
Keywords	Escherichia coli ; chromates ; imports ; mutants ; oxyanions ; phosphates ; research ; sulfates ; toxicity
Language	English
Dates of publication	2022-0524
Publishing place	Elsevier Masson SAS
Document type	Article
Note	Pre-press version
ZDB-ID	1004220-9
ISSN	1769-7123 ; 0923-2508
ISSN (online)	1769-7123
ISSN	0923-2508
DOI	10.1016/j.resmic.2022.103967
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Article ; Online: Iron limitation indirectly reduces the

Hasnat, Muhammad Abrar / Zupok, Arkadiusz / Gorka, Michal / Iobbi-Nivol, Chantal / Skirycz, Aleksandra / Jourlin-Castelli, Cécile / Bier, Frank / Agarwal, Saloni / Irefo, Ehizode / Leimkühler, Silke

Microbiology spectrum

2024 Volume 12, Issue 2, Page(s) e0348023

Abstract: The expression of most molybdoenzymes ... ...

Abstract	The expression of most molybdoenzymes in
MeSH term(s)	Escherichia coli/genetics ; Iron/metabolism ; Operon ; Escherichia coli Proteins/genetics ; Transcription Factors/metabolism ; Oxidoreductases/genetics ; Molybdenum Cofactors ; Oxides/metabolism ; Anaerobiosis ; Bacterial Proteins/genetics ; Gene Expression Regulation, Bacterial ; Methylamines
Chemical Substances	trimethylamine (LHH7G8O305) ; Iron (E1UOL152H7) ; Escherichia coli Proteins ; Transcription Factors ; Oxidoreductases (EC 1.-) ; Molybdenum Cofactors ; Oxides ; Bacterial Proteins ; Methylamines
Language	English
Publishing date	2024-01-09
Publishing country	United States
Document type	Journal Article
ZDB-ID	2807133-5
ISSN	2165-0497 ; 2165-0497
ISSN (online)	2165-0497
ISSN	2165-0497
DOI	10.1128/spectrum.03480-23
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Article ; Online: Electrochemical Trimethylamine

Waffo, Armel F T / Mitrova, Biljana / Tiedemann, Kim / Iobbi-Nivol, Chantal / Leimkühler, Silke / Wollenberger, Ulla

Biosensors

2021 Volume 11, Issue 4

Abstract: An amperometric ... ...

Abstract	An amperometric trimethylamine
MeSH term(s)	Biosensing Techniques ; Electrodes ; Escherichia coli ; Glucose Oxidase ; Humans ; Methylamines/analysis ; Oxygen
Chemical Substances	Methylamines ; Glucose Oxidase (EC 1.1.3.4) ; trimethyloxamine (FLD0K1SJ1A) ; Oxygen (S88TT14065)
Language	English
Publishing date	2021-03-27
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2662125-3
ISSN	2079-6374 ; 2079-6374
ISSN (online)	2079-6374
ISSN	2079-6374
DOI	10.3390/bios11040098
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Article ; Online: Reconstitution of Molybdoenzymes with Bis-Molybdopterin Guanine Dinucleotide Cofactors.

Kaufmann, Paul / Iobbi-Nivol, Chantal / Leimkühler, Silke

Methods in molecular biology (Clifton, N.J.)

2018 Volume 1876, Page(s) 141–152

Abstract: Molybdoenzymes are ubiquitous and play important roles in all kingdoms of life. The cofactors of these enzymes comprise the metal, molybdenum (Mo), which is bound to a special organic ligand system called molybdopterin (MPT). Additional small ligands are ...

Abstract	Molybdoenzymes are ubiquitous and play important roles in all kingdoms of life. The cofactors of these enzymes comprise the metal, molybdenum (Mo), which is bound to a special organic ligand system called molybdopterin (MPT). Additional small ligands are present at the Mo atom, including water, hydroxide, oxo-, sulfido-, or selenido-functionalities, and in some enzymes, amino acid ligand, such as serine, aspartate, cysteine, or selenocysteine that coordinate the cofactor to the peptide chain of the enzyme. The so-called molybdenum cofactor (Moco) is deeply buried within the protein at the end of a narrow funnel, giving access only to the substrate. In 1974, an assay was developed by Nason and coworkers using the pleiotropic Neurospora crassa mutant, nit-1, for the reconstitution of molybdoenzyme activities from crude extracts. These studies have led to the understanding that Moco is the common element in all molybdoenzymes from different organisms. The assay has been further developed since then by using specific molybdenum enzymes as the source of Moco for the reconstitution of diverse purified apo-molybdoenzymes. Alternatively, the molybdenum cofactor can be synthesized in vitro from stable intermediates and subsequently inserted into apo-molybdoenzymes with the assistance of specific Moco-binding chaperones. A general working protocol is described here for the insertion of the bis-molybdopterin guanine dinucleotide cofactor (bis-MGD) into its target molybdoenzyme using the example of Escherichia coli trimethylamine N-oxide (TMAO) reductase.
MeSH term(s)	Guanine Nucleotides/chemistry ; Metalloproteins/chemistry ; Metalloproteins/metabolism ; Molecular Structure ; Molybdenum/chemistry ; Oxidation-Reduction ; Pterins/chemistry
Chemical Substances	Guanine Nucleotides ; Metalloproteins ; Pterins ; molybdopterin guanine dinucleotide (128007-95-4) ; Molybdenum (81AH48963U)
Language	English
Publishing date	2018-10-13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-8864-8_9
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Article ; Online: Bacterial molybdoenzymes: old enzymes for new purposes.

Leimkühler, Silke / Iobbi-Nivol, Chantal

FEMS microbiology reviews

2015 Volume 40, Issue 1, Page(s) 1–18

Abstract: Molybdoenzymes are widespread in eukaryotic and prokaryotic organisms where they play crucial functions in detoxification reactions in the metabolism of humans and bacteria, in nitrate assimilation in plants and in anaerobic respiration in bacteria. To ... ...

Abstract	Molybdoenzymes are widespread in eukaryotic and prokaryotic organisms where they play crucial functions in detoxification reactions in the metabolism of humans and bacteria, in nitrate assimilation in plants and in anaerobic respiration in bacteria. To be fully active, these enzymes require complex molybdenum-containing cofactors, which are inserted into the apoenzymes after folding. For almost all the bacterial molybdoenzymes, molybdenum cofactor insertion requires the involvement of specific chaperones. In this review, an overview on the molybdenum cofactor biosynthetic pathway is given together with the role of specific chaperones dedicated for molybdenum cofactor insertion and maturation. Many bacteria are involved in geochemical cycles on earth and therefore have an environmental impact. The roles of molybdoenzymes in bioremediation and for environmental applications are presented.
MeSH term(s)	Apoenzymes/metabolism ; Bacteria/enzymology ; Bacterial Proteins/metabolism ; Coenzymes/biosynthesis ; Coenzymes/metabolism ; Environmental Microbiology ; Metalloproteins/biosynthesis ; Metalloproteins/metabolism ; Molecular Chaperones/metabolism ; Pteridines/metabolism
Chemical Substances	Apoenzymes ; Bacterial Proteins ; Coenzymes ; Metalloproteins ; Molecular Chaperones ; Pteridines ; molybdenum cofactor (ATN6EG42UQ)
Language	English
Publishing date	2015-10-13
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	283740-7
ISSN	1574-6976 ; 0168-6445
ISSN (online)	1574-6976
ISSN	0168-6445
DOI	10.1093/femsre/fuv043
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Article ; Online: The Tol-Pal system of Escherichia coli plays an unexpected role in the import of the oxyanions chromate and phosphate.

Ali Chaouche, Amine / Houot, Laetitia / Duché, Denis / Iobbi-Nivol, Chantal / Giudici-Orticoni, Marie-Thérèse / Fons, Michel / Méjean, Vincent

Research in microbiology

2022 Volume 173, Issue 8, Page(s) 103967

Abstract	Chromate is a toxic metal that enters bacteria by using oxyanion importers. Here, we show that each mutant of the Tol-Pal system of Escherichia coli exhibited increased chromate resistance. This system, which spans the cell envelope, plays a major role in envelope integrity and septation. The ΔtolQR mutant accumulated three-fold less chromate than the wild-type. Addition of phosphate but not sulfate to rich medium drastically reduced chromate toxicity and import in the wild-type strain. Furthermore, the intracellular concentration of free inorganic phosphate was significantly reduced for the ΔtolR mutant in comparison to the wild-type strain. Moreover, extracellular labeled phosphate was significantly less incorporated into the ΔtolR mutant. Finally, two distinct TolQR mutant complexes, specifically affected in Tol-Pal energization without affecting the TolQRA complex structure, did not complement the ΔtolQR mutant for inorganic phosphate accumulation. We thus propose that, while the Pst system is well known to import inorganic phosphate, the Tol-Pal system participates to phosphate uptake in particular at medium to high extracellular phosphate concentrations. Since mutations disabling the Tol-Pal system lead to pleiotropic effects, chromate resistance and reduced inorganic phosphate import could occur from an indirect effect of mutations in components of the Tol-Pal system.
MeSH term(s)	Escherichia coli/genetics ; Escherichia coli Proteins/genetics ; Chromates ; Phosphates
Chemical Substances	Escherichia coli Proteins ; Chromates ; Phosphates
Language	English
Publishing date	2022-06-01
Publishing country	France
Document type	Journal Article
ZDB-ID	1004220-9
ISSN	1769-7123 ; 0923-2508
ISSN (online)	1769-7123
ISSN	0923-2508
DOI	10.1016/j.resmic.2022.103967
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Zs.A 890: Show issues

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Article ; Online: The regulation of Moco biosynthesis and molybdoenzyme gene expression by molybdenum and iron in bacteria.

Zupok, Arkadiusz / Iobbi-Nivol, Chantal / Méjean, Vincent / Leimkühler, Silke

Metallomics : integrated biometal science

2019 Volume 11, Issue 10, Page(s) 1602–1624

Abstract: Bacterial molybdoenzymes are key enzymes involved in the global sulphur, nitrogen and carbon cycles. These enzymes require the insertion of the molybdenum cofactor (Moco) into their active sites and are able to catalyse a large range of redox-reactions. ... ...

Abstract	Bacterial molybdoenzymes are key enzymes involved in the global sulphur, nitrogen and carbon cycles. These enzymes require the insertion of the molybdenum cofactor (Moco) into their active sites and are able to catalyse a large range of redox-reactions. Escherichia coli harbours nineteen different molybdoenzymes that require a tight regulation of their synthesis according to substrate availability, oxygen availability and the cellular concentration of molybdenum and iron. The synthesis and assembly of active molybdoenzymes are regulated at the level of transcription of the structural genes and of translation in addition to the genes involved in Moco biosynthesis. The action of global transcriptional regulators like FNR, NarXL/QP, Fur and ArcA and their roles on the expression of these genes is described in detail. In this review we focus on what is known about the molybdenum- and iron-dependent regulation of molybdoenzyme and Moco biosynthesis genes in the model organism E. coli. The gene regulation in E. coli is compared to two other well studied model organisms Rhodobacter capsulatus and Shewanella oneidensis.
MeSH term(s)	Bacteria/genetics ; Bacteria/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Biosynthetic Pathways ; Coenzymes/genetics ; Coenzymes/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Gene Expression Regulation, Bacterial ; Genes, Bacterial ; Iron/metabolism ; Metalloproteins/genetics ; Metalloproteins/metabolism ; Molybdenum/metabolism ; Multigene Family ; Pteridines/metabolism ; Rhodobacter capsulatus/genetics ; Rhodobacter capsulatus/metabolism ; Shewanella/genetics ; Shewanella/metabolism
Chemical Substances	Bacterial Proteins ; Coenzymes ; Metalloproteins ; Pteridines ; Molybdenum (81AH48963U) ; molybdenum cofactor (ATN6EG42UQ) ; Iron (E1UOL152H7)
Language	English
Publishing date	2019-09-04
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2474317-3
ISSN	1756-591X ; 1756-5901
ISSN (online)	1756-591X
ISSN	1756-5901
DOI	10.1039/c9mt00186g
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Article ; Online: Same but different: Comparison of two system-specific molecular chaperones for the maturation of formate dehydrogenases.

Schwanhold, Nadine / Iobbi-Nivol, Chantal / Lehmann, Angelika / Leimkühler, Silke

PloS one

2018 Volume 13, Issue 11, Page(s) e0201935

Abstract: The maturation of bacterial molybdoenzymes is a complex process leading to the insertion of the bulky bis-molybdopterin guanine dinucleotide (bis-MGD) cofactor into the apo-enzyme. Most molybdoenzymes were shown to contain a specific chaperone for the ... ...

Abstract	The maturation of bacterial molybdoenzymes is a complex process leading to the insertion of the bulky bis-molybdopterin guanine dinucleotide (bis-MGD) cofactor into the apo-enzyme. Most molybdoenzymes were shown to contain a specific chaperone for the insertion of the bis-MGD cofactor. Formate dehydrogenases (FDH) together with their molecular chaperone partner seem to display an exception to this specificity rule, since the chaperone FdhD has been proven to be involved in the maturation of all three FDH enzymes present in Escherichia coli. Multiple roles have been suggested for FdhD-like chaperones in the past, including the involvement in a sulfur transfer reaction from the l-cysteine desulfurase IscS to bis-MGD by the action of two cysteine residues present in a conserved CXXC motif of the chaperones. However, in this study we show by phylogenetic analyses that the CXXC motif is not conserved among FdhD-like chaperones. We compared in detail the FdhD-like homologues from Rhodobacter capsulatus and E. coli and show that their roles in the maturation of FDH enzymes from different subgroups can be exchanged. We reveal that bis-MGD-binding is a common characteristic of FdhD-like proteins and that the cofactor is bound with a sulfido-ligand at the molybdenum atom to the chaperone. Generally, we reveal that the cysteine residues in the motif CXXC of the chaperone are not essential for the production of active FDH enzymes.
MeSH term(s)	Amino Acid Motifs ; Escherichia coli/chemistry ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Formate Dehydrogenases/chemistry ; Formate Dehydrogenases/genetics ; Formate Dehydrogenases/metabolism ; Molecular Chaperones/chemistry ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Rhodobacter capsulatus/chemistry ; Rhodobacter capsulatus/genetics
Chemical Substances	Escherichia coli Proteins ; Molecular Chaperones ; Formate Dehydrogenases (EC 1.2.1.2)
Language	English
Publishing date	2018-11-16
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0201935
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